HEADER ISOMERASE 19-AUG-04 1X94
TITLE CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PHOSPHOHEPTOSE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 GENE: LPCA, GMHA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYPOTHETICAL PROTEIN, VIBRIO CHOLERAE, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, NYSGXRC, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SEETHARAMAN,S.SWAMINATHAN,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 7 14-FEB-24 1X94 1 REMARK
REVDAT 6 03-FEB-21 1X94 1 AUTHOR JRNL
REVDAT 5 09-FEB-11 1X94 1 AUTHOR
REVDAT 4 24-FEB-09 1X94 1 VERSN
REVDAT 3 01-MAY-07 1X94 1 AUTHOR
REVDAT 2 24-OCT-06 1X94 1 HEADER KEYWDS AUTHOR REMARK
REVDAT 2 2 1 DBREF MASTER
REVDAT 1 14-SEP-04 1X94 0
JRNL AUTH J.SEETHARAMAN,K.R.RAJASHANKAR,V.SOLORZANO,R.KNIEWEL,
JRNL AUTH 2 C.D.LIMA,J.B.BONANNO,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURES OF TWO PUTATIVE PHOSPHOHEPTOSE
JRNL TITL 2 ISOMERASES.
JRNL REF PROTEINS V. 63 1092 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16477602
JRNL DOI 10.1002/PROT.20908
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 206203.500
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 13018
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) : 0.229
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1304
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1796
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 194
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 68
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.10000
REMARK 3 B22 (A**2) : 2.93000
REMARK 3 B33 (A**2) : 7.17000
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) : 0.33
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) : 0.46
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.720
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) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 51.99
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ELECTRON DENSITY WAS ABSENT OR WEAK
REMARK 3 FOR THE MISSING RESIDUES.
REMARK 4
REMARK 4 1X94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000030094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97862,0.97904,0.94
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS - B4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CBASS
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18477
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, BIS TRIS, NACL, PH
REMARK 280 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 20K, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 67.13950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.05600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 67.13950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.05600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 134.27900
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 SER A 83
REMARK 465 ASP A 84
REMARK 465 PRO A 85
REMARK 465 SER A 86
REMARK 465 HIS A 87
REMARK 465 LEU A 88
REMARK 465 SER A 89
REMARK 465 CYS A 90
REMARK 465 VAL A 91
REMARK 465 SER A 92
REMARK 465 ASN A 93
REMARK 465 ASP A 94
REMARK 465 PHE A 95
REMARK 465 GLY A 96
REMARK 465 TYR A 97
REMARK 465 SER B 83
REMARK 465 ASP B 84
REMARK 465 PRO B 85
REMARK 465 SER B 86
REMARK 465 HIS B 87
REMARK 465 LEU B 88
REMARK 465 SER B 89
REMARK 465 CYS B 90
REMARK 465 VAL B 91
REMARK 465 SER B 92
REMARK 465 ASN B 93
REMARK 465 ASP B 94
REMARK 465 PHE B 95
REMARK 465 GLY B 96
REMARK 465 TYR B 97
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 TYR A 2 -25.63 -166.84
REMARK 500 LYS A 147 -123.05 60.20
REMARK 500 MET A 190 67.03 -155.44
REMARK 500 TYR B 70 -3.78 -140.68
REMARK 500 ASN B 73 80.52 52.63
REMARK 500 ARG B 74 125.56 174.11
REMARK 500 LYS B 147 -123.90 45.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T1485 RELATED DB: TARGETDB
DBREF 1X94 A 1 191 UNP Q9KPY2 GMHA_VIBCH 1 191
DBREF 1X94 B 1 191 UNP Q9KPY2 GMHA_VIBCH 1 191
SEQRES 1 A 191 MET TYR GLN ASP LEU ILE ARG SER GLU LEU THR GLU ALA
SEQRES 2 A 191 ALA ASP VAL LEU GLN LYS PHE LEU SER ASP ASP HIS ASN
SEQRES 3 A 191 ILE ALA GLN ILE GLU ALA ALA ALA LYS LEU ILE ALA ASP
SEQRES 4 A 191 SER PHE LYS GLN GLY GLY LYS VAL LEU SER CYS GLY ASN
SEQRES 5 A 191 GLY GLY SER HIS CYS ASP ALA MET HIS PHE ALA GLU GLU
SEQRES 6 A 191 LEU THR GLY ARG TYR ARG GLU ASN ARG PRO GLY TYR PRO
SEQRES 7 A 191 GLY ILE ALA ILE SER ASP PRO SER HIS LEU SER CYS VAL
SEQRES 8 A 191 SER ASN ASP PHE GLY TYR ASP TYR VAL PHE SER ARG TYR
SEQRES 9 A 191 VAL GLU ALA VAL GLY ALA LYS GLY ASP VAL LEU PHE GLY
SEQRES 10 A 191 LEU SER THR SER GLY ASN SER GLY ASN ILE LEU LYS ALA
SEQRES 11 A 191 ILE GLU ALA ALA LYS ALA LYS GLY MET LYS THR ILE ALA
SEQRES 12 A 191 LEU THR GLY LYS ASP GLY GLY LYS MET ALA GLY LEU ALA
SEQRES 13 A 191 ASP VAL GLU ILE ARG VAL PRO HIS PHE GLY TYR ALA ASP
SEQRES 14 A 191 ARG ILE GLN GLU VAL HIS ILE LYS ILE ILE HIS ILE ILE
SEQRES 15 A 191 ILE GLN LEU ILE GLU LYS GLU MET ALA
SEQRES 1 B 191 MET TYR GLN ASP LEU ILE ARG SER GLU LEU THR GLU ALA
SEQRES 2 B 191 ALA ASP VAL LEU GLN LYS PHE LEU SER ASP ASP HIS ASN
SEQRES 3 B 191 ILE ALA GLN ILE GLU ALA ALA ALA LYS LEU ILE ALA ASP
SEQRES 4 B 191 SER PHE LYS GLN GLY GLY LYS VAL LEU SER CYS GLY ASN
SEQRES 5 B 191 GLY GLY SER HIS CYS ASP ALA MET HIS PHE ALA GLU GLU
SEQRES 6 B 191 LEU THR GLY ARG TYR ARG GLU ASN ARG PRO GLY TYR PRO
SEQRES 7 B 191 GLY ILE ALA ILE SER ASP PRO SER HIS LEU SER CYS VAL
SEQRES 8 B 191 SER ASN ASP PHE GLY TYR ASP TYR VAL PHE SER ARG TYR
SEQRES 9 B 191 VAL GLU ALA VAL GLY ALA LYS GLY ASP VAL LEU PHE GLY
SEQRES 10 B 191 LEU SER THR SER GLY ASN SER GLY ASN ILE LEU LYS ALA
SEQRES 11 B 191 ILE GLU ALA ALA LYS ALA LYS GLY MET LYS THR ILE ALA
SEQRES 12 B 191 LEU THR GLY LYS ASP GLY GLY LYS MET ALA GLY LEU ALA
SEQRES 13 B 191 ASP VAL GLU ILE ARG VAL PRO HIS PHE GLY TYR ALA ASP
SEQRES 14 B 191 ARG ILE GLN GLU VAL HIS ILE LYS ILE ILE HIS ILE ILE
SEQRES 15 B 191 ILE GLN LEU ILE GLU LYS GLU MET ALA
FORMUL 3 HOH *68(H2 O)
HELIX 1 1 TYR A 2 SER A 22 1 21
HELIX 2 2 ASP A 23 LYS A 42 1 20
HELIX 3 3 GLY A 54 ARG A 71 1 18
HELIX 4 4 TYR A 99 GLY A 109 1 11
HELIX 5 5 SER A 124 GLY A 138 1 15
HELIX 6 6 GLY A 149 ALA A 153 5 5
HELIX 7 7 TYR A 167 MET A 190 1 24
HELIX 8 8 TYR B 2 ASP B 23 1 22
HELIX 9 9 ASP B 23 GLN B 43 1 21
HELIX 10 10 SER B 55 ARG B 71 1 17
HELIX 11 11 TYR B 99 GLY B 109 1 11
HELIX 12 12 SER B 124 ALA B 136 1 13
HELIX 13 13 GLY B 149 ALA B 153 5 5
HELIX 14 14 TYR B 167 ALA B 191 1 25
SHEET 1 A 5 GLY A 79 ALA A 81 0
SHEET 2 A 5 VAL A 47 CYS A 50 1 N VAL A 47 O ILE A 80
SHEET 3 A 5 VAL A 114 SER A 119 1 O PHE A 116 N LEU A 48
SHEET 4 A 5 LYS A 140 GLY A 146 1 O ILE A 142 N GLY A 117
SHEET 5 A 5 VAL A 158 VAL A 162 1 O ILE A 160 N ALA A 143
SHEET 1 B 5 GLY B 79 ALA B 81 0
SHEET 2 B 5 VAL B 47 GLY B 51 1 N VAL B 47 O ILE B 80
SHEET 3 B 5 VAL B 114 SER B 119 1 O VAL B 114 N LEU B 48
SHEET 4 B 5 LYS B 140 THR B 145 1 O LEU B 144 N SER B 119
SHEET 5 B 5 VAL B 158 ARG B 161 1 O ILE B 160 N THR B 145
CRYST1 134.279 46.112 60.350 90.00 90.00 90.00 P 21 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 0.007447 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021686 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016570 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
