HEADER MEMBRANE PROTEIN 18-JAN-07 2OL6
TITLE THE CRYSTAL STRUCTURE OF OSPA MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OUTER SURFACE PROTEIN A;
COMPND 3 CHAIN: O;
COMPND 4 FRAGMENT: RESIDUES 27-273;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;
SOURCE 3 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;
SOURCE 4 ORGANISM_TAXID: 139;
SOURCE 5 GENE: OSPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS BETA-SHEET, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MAKABE,V.TERECHKO,S.KOIDE
REVDAT 4 30-AUG-23 2OL6 1 REMARK
REVDAT 3 20-OCT-21 2OL6 1 SEQADV
REVDAT 2 24-FEB-09 2OL6 1 VERSN
REVDAT 1 11-DEC-07 2OL6 0
JRNL AUTH K.MAKABE,S.YAN,V.TERESHKO,G.GAWLAK,S.KOIDE
JRNL TITL BETA-STRAND FLIPPING AND SLIPPING TRIGGERED BY TURN
JRNL TITL 2 REPLACEMENT REVEAL THE OPPORTUNISTIC NATURE OF BETA-STRAND
JRNL TITL 3 PAIRING
JRNL REF J.AM.CHEM.SOC. V. 129 14661 2007
JRNL REFN ISSN 0002-7863
JRNL PMID 17985889
JRNL DOI 10.1021/JA074252C
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 26475
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1427
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1922
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1800
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.23000
REMARK 3 B22 (A**2) : 1.94000
REMARK 3 B33 (A**2) : -3.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.47000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.479
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1818 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1661 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2455 ; 1.569 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3926 ; 0.764 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ; 5.727 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 60 ;36.667 ;28.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 357 ;14.898 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;12.184 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 312 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2000 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 289 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 269 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1594 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 923 ; 0.164 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1167 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 138 ; 0.172 ; 0.200
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): 29 ; 0.169 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 61 ; 0.275 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.244 ; 0.200
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): 1544 ; 1.214 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 514 ; 0.287 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1961 ; 1.493 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 675 ; 2.782 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 492 ; 3.998 ; 4.500
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 : BABINET MODEL WITH 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 2OL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041273.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28159
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.960
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2G8C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG400, 4% MPD, AND 100MM
REMARK 280 IMIDAZOLE, PH 7.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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,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 25.75400
REMARK 290 SMTRY3 2 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 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 APPLY THE FOLLOWING TO CHAINS: 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 GLY O 23
REMARK 465 SER O 24
REMARK 465 HIS O 25
REMARK 465 MET O 26
REMARK 465 LYS O 27
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 O 59 -125.41 53.68
REMARK 500 ALA O 83 -2.75 85.93
REMARK 500 THR O 252 -45.64 -133.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OL7 RELATED DB: PDB
REMARK 900 RELATED ID: 2OL8 RELATED DB: PDB
DBREF 2OL6 O 27 272 UNP Q45040 Q45040_BORBU 27 273
SEQADV 2OL6 GLY O 23 UNP Q45040 EXPRESSION TAG
SEQADV 2OL6 SER O 24 UNP Q45040 EXPRESSION TAG
SEQADV 2OL6 HIS O 25 UNP Q45040 EXPRESSION TAG
SEQADV 2OL6 MET O 26 UNP Q45040 EXPRESSION TAG
SEQADV 2OL6 SER O 37 UNP Q45040 GLU 37 ENGINEERED MUTATION
SEQADV 2OL6 SER O 45 UNP Q45040 GLU 45 ENGINEERED MUTATION
SEQADV 2OL6 SER O 46 UNP Q45040 LYS 46 ENGINEERED MUTATION
SEQADV 2OL6 ALA O 48 UNP Q45040 LYS 48 ENGINEERED MUTATION
SEQADV 2OL6 ALA O 60 UNP Q45040 LYS 60 ENGINEERED MUTATION
SEQADV 2OL6 SER O 64 UNP Q45040 LYS 64 ENGINEERED MUTATION
SEQADV 2OL6 ALA O 83 UNP Q45040 LYS 83 ENGINEERED MUTATION
SEQADV 2OL6 SER O 104 UNP Q45040 GLU 104 ENGINEERED MUTATION
SEQADV 2OL6 SER O 107 UNP Q45040 LYS 107 ENGINEERED MUTATION
SEQADV 2OL6 ASN O 117 UNP Q45040 LYS 117 ENGINEERED MUTATION
SEQADV 2OL6 GLY O 118 UNP Q45040 ASP 118 ENGINEERED MUTATION
SEQADV 2OL6 O UNP Q45040 LYS 119 DELETION
SEQADV 2OL6 SER O 238 UNP Q45040 LYS 239 ENGINEERED MUTATION
SEQADV 2OL6 SER O 239 UNP Q45040 GLU 240 ENGINEERED MUTATION
SEQADV 2OL6 SER O 253 UNP Q45040 LYS 254 ENGINEERED MUTATION
SEQRES 1 O 250 GLY SER HIS MET LYS ASN SER VAL SER VAL ASP LEU PRO
SEQRES 2 O 250 GLY SER MET LYS VAL LEU VAL SER LYS SER SER ASN ALA
SEQRES 3 O 250 ASP GLY LYS TYR ASP LEU ILE ALA THR VAL ASP ALA LEU
SEQRES 4 O 250 GLU LEU SER GLY THR SER ASP LYS ASN ASN GLY SER GLY
SEQRES 5 O 250 VAL LEU GLU GLY VAL LYS ALA ASP ALA SER LYS VAL LYS
SEQRES 6 O 250 LEU THR ILE SER ASP ASP LEU GLY GLN THR THR LEU GLU
SEQRES 7 O 250 VAL PHE LYS SER ASP GLY SER THR LEU VAL SER LYS LYS
SEQRES 8 O 250 VAL THR SER ASN GLY SER SER THR GLU GLU LYS PHE ASN
SEQRES 9 O 250 GLU LYS GLY GLU VAL SER GLU LYS ILE ILE THR ARG ALA
SEQRES 10 O 250 ASP GLY THR ARG LEU GLU TYR THR GLY ILE LYS SER ASP
SEQRES 11 O 250 GLY SER GLY LYS ALA LYS GLU VAL LEU LYS GLY TYR VAL
SEQRES 12 O 250 LEU GLU GLY THR LEU THR ALA GLU LYS THR THR LEU VAL
SEQRES 13 O 250 VAL LYS GLU GLY THR VAL THR LEU SER LYS ASN ILE SER
SEQRES 14 O 250 LYS SER GLY GLU VAL SER VAL GLU LEU ASN ASP THR ASP
SEQRES 15 O 250 SER SER ALA ALA THR LYS LYS THR ALA ALA TRP ASN SER
SEQRES 16 O 250 GLY THR SER THR LEU THR ILE THR VAL ASN SER LYS LYS
SEQRES 17 O 250 THR LYS ASP LEU VAL PHE THR SER SER ASN THR ILE THR
SEQRES 18 O 250 VAL GLN GLN TYR ASP SER ASN GLY THR SER LEU GLU GLY
SEQRES 19 O 250 SER ALA VAL GLU ILE THR LYS LEU ASP GLU ILE LYS ASN
SEQRES 20 O 250 ALA LEU LYS
FORMUL 2 HOH *175(H2 O)
HELIX 1 1 LYS O 263 LEU O 271 1 9
SHEET 1 A16 SER O 29 LEU O 34 0
SHEET 2 A16 MET O 38 SER O 43 -1 O VAL O 42 N VAL O 30
SHEET 3 A16 TYR O 52 VAL O 58 -1 O ILE O 55 N LEU O 41
SHEET 4 A16 LEU O 61 SER O 67 -1 O LEU O 63 N ALA O 56
SHEET 5 A16 GLY O 74 VAL O 79 -1 O GLU O 77 N SER O 64
SHEET 6 A16 LYS O 85 ILE O 90 -1 O ILE O 90 N GLY O 74
SHEET 7 A16 GLN O 96 PHE O 102 -1 O PHE O 102 N LYS O 85
SHEET 8 A16 LEU O 109 SER O 116 -1 O VAL O 110 N VAL O 101
SHEET 9 A16 SER O 119 PHE O 125 -1 O GLU O 123 N LYS O 112
SHEET 10 A16 VAL O 131 THR O 137 -1 O ILE O 135 N GLU O 122
SHEET 11 A16 ARG O 143 THR O 147 -1 O TYR O 146 N LYS O 134
SHEET 12 A16 GLY O 155 LEU O 161 -1 O VAL O 160 N ARG O 143
SHEET 13 A16 TYR O 164 LEU O 170 -1 O LEU O 166 N GLU O 159
SHEET 14 A16 LYS O 174 GLU O 181 -1 O THR O 176 N THR O 169
SHEET 15 A16 VAL O 184 SER O 191 -1 O LYS O 188 N LEU O 177
SHEET 16 A16 VAL O 196 ASP O 202 -1 O SER O 197 N ASN O 189
SHEET 1 B 5 LYS O 211 ASN O 216 0
SHEET 2 B 5 THR O 221 VAL O 226 -1 O THR O 225 N THR O 212
SHEET 3 B 5 LYS O 229 PHE O 236 -1 O THR O 231 N ILE O 224
SHEET 4 B 5 ILE O 242 GLN O 246 -1 O GLN O 245 N ASP O 233
SHEET 5 B 5 VAL O 259 GLU O 260 -1 O VAL O 259 N VAL O 244
CRYST1 32.882 51.508 65.639 90.00 98.56 90.00 P 1 21 1 2
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 0.030412 0.000000 0.004579 0.00000
SCALE2 0.000000 0.019414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015407 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
