HEADER SUGAR BINDING PROTEIN 21-MAY-03 1PEB
TITLE LIGAND-FREE HIGH-AFFINITY MALTOSE-BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOSE-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MALTODEXTRIN-BINDING PROTEIN, MMBP;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: MALE OR B4034 OR Z5632 OR ECS5017;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HS3309;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PLH1
KEYWDS MBP, MALTOSE-BINDING PROTEIN, HIGH-AFFINITY MUTANT, ENGINEERED, SUGAR
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.G.TELMER,B.H.SHILTON
REVDAT 6 16-AUG-23 1PEB 1 REMARK
REVDAT 5 27-OCT-21 1PEB 1 SEQADV
REVDAT 4 11-OCT-17 1PEB 1 REMARK
REVDAT 3 24-FEB-09 1PEB 1 VERSN
REVDAT 2 09-SEP-03 1PEB 1 JRNL
REVDAT 1 12-AUG-03 1PEB 0
JRNL AUTH P.G.TELMER,B.H.SHILTON
JRNL TITL INSIGHTS INTO THE CONFORMATIONAL EQUILIBRIA OF
JRNL TITL 2 MALTOSE-BINDING PROTEIN BY ANALYSIS OF HIGH AFFINITY
JRNL TITL 3 MUTANTS.
JRNL REF J.BIOL.CHEM. V. 278 34555 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12794084
JRNL DOI 10.1074/JBC.M301004200
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.88
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) (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 10198
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) : 0.181
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1051
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1603
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2833
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.42000
REMARK 3 B22 (A**2) : 6.38000
REMARK 3 B33 (A**2) : -0.96000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.49000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.42
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.900
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) : 1.900 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.700 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.090 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 33.16
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 5 : MALTOSE.PARA
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESOLUTION-DEPENDENT WEIGHTING SCHEME,
REMARK 3 BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1PEB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : GRADED MULTILAYER (OSMIC)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10346
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05300
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1MPB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3500, CACODYLIC ACID, ZINC
REMARK 280 ACETATE, SODIUM CHLORIDE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 312K
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 35.17500
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: 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 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 55 -168.73 -115.71
REMARK 500 ALA A 168 -106.52 -67.32
REMARK 500 TYR A 171 97.73 -39.41
REMARK 500 ASP A 209 -161.16 -115.66
REMARK 500 LYS A 239 -8.76 75.67
REMARK 500 TYR A 283 -51.19 -120.42
REMARK 500 PRO A 331 108.66 -47.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1N3W RELATED DB: PDB
REMARK 900 RELATED ID: 1N3X RELATED DB: PDB
REMARK 900 RELATED ID: 1NL5 RELATED DB: PDB
DBREF 1PEB A 1 370 UNP P02928 MALE_ECOLI 27 396
SEQADV 1PEB A UNP P02928 GLU 198 DELETION
SEQADV 1PEB A UNP P02928 ASN 199 DELETION
SEQADV 1PEB A UNP P02928 LYS 201 DELETION
SEQADV 1PEB A UNP P02928 TYR 202 DELETION
SEQADV 1PEB ALA A 321 UNP P02928 MET 347 ENGINEERED MUTATION
SEQADV 1PEB ALA A 325 UNP P02928 GLN 351 ENGINEERED MUTATION
SEQRES 1 A 366 LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY
SEQRES 2 A 366 ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS
SEQRES 3 A 366 PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS
SEQRES 4 A 366 PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA
SEQRES 5 A 366 THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP
SEQRES 6 A 366 ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU
SEQRES 7 A 366 ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU TYR PRO
SEQRES 8 A 366 PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE
SEQRES 9 A 366 ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR
SEQRES 10 A 366 ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU
SEQRES 11 A 366 GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY
SEQRES 12 A 366 LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE
SEQRES 13 A 366 THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE
SEQRES 14 A 366 LYS TYR GLY ASP ILE LYS ASP VAL GLY VAL ASP ASN ALA
SEQRES 15 A 366 GLY ALA LYS ALA GLY LEU THR PHE LEU VAL ASP LEU ILE
SEQRES 16 A 366 LYS ASN LYS HIS MET ASN ALA ASP THR ASP TYR SER ILE
SEQRES 17 A 366 ALA GLU ALA ALA PHE ASN LYS GLY GLU THR ALA MET THR
SEQRES 18 A 366 ILE ASN GLY PRO TRP ALA TRP SER ASN ILE ASP THR SER
SEQRES 19 A 366 LYS VAL ASN TYR GLY VAL THR VAL LEU PRO THR PHE LYS
SEQRES 20 A 366 GLY GLN PRO SER LYS PRO PHE VAL GLY VAL LEU SER ALA
SEQRES 21 A 366 GLY ILE ASN ALA ALA SER PRO ASN LYS GLU LEU ALA LYS
SEQRES 22 A 366 GLU PHE LEU GLU ASN TYR LEU LEU THR ASP GLU GLY LEU
SEQRES 23 A 366 GLU ALA VAL ASN LYS ASP LYS PRO LEU GLY ALA VAL ALA
SEQRES 24 A 366 LEU LYS SER TYR GLU GLU GLU LEU ALA LYS ASP PRO ARG
SEQRES 25 A 366 ILE ALA ALA THR ALA GLU ASN ALA ALA LYS GLY GLU ILE
SEQRES 26 A 366 MET PRO ASN ILE PRO GLN MET SER ALA PHE TRP TYR ALA
SEQRES 27 A 366 VAL ARG THR ALA VAL ILE ASN ALA ALA SER GLY ARG GLN
SEQRES 28 A 366 THR VAL ASP GLU ALA LEU LYS ASP ALA GLN THR ARG ILE
SEQRES 29 A 366 THR LYS
FORMUL 2 HOH *91(H2 O)
HELIX 1 1 GLY A 16 GLY A 32 1 17
HELIX 2 2 LYS A 42 ALA A 51 1 10
HELIX 3 3 ALA A 52 GLY A 54 5 3
HELIX 4 4 ARG A 66 SER A 73 1 8
HELIX 5 5 ASP A 82 ASP A 87 1 6
HELIX 6 6 TYR A 90 ALA A 96 1 7
HELIX 7 7 GLU A 131 ALA A 141 1 11
HELIX 8 8 GLU A 153 ALA A 162 1 10
HELIX 9 9 ASN A 185 ASN A 201 1 17
HELIX 10 10 ASP A 209 LYS A 219 1 11
HELIX 11 11 GLY A 228 TRP A 230 5 3
HELIX 12 12 ALA A 231 SER A 238 1 8
HELIX 13 13 ASN A 272 TYR A 283 1 12
HELIX 14 14 THR A 286 LYS A 297 1 12
HELIX 15 15 LEU A 304 ALA A 312 1 9
HELIX 16 16 ASP A 314 LYS A 326 1 13
HELIX 17 17 GLN A 335 SER A 352 1 18
HELIX 18 18 THR A 356 LYS A 370 1 15
SHEET 1 A 6 LYS A 34 GLU A 38 0
SHEET 2 A 6 LYS A 6 TRP A 10 1 N ILE A 9 O THR A 36
SHEET 3 A 6 ILE A 59 ALA A 63 1 O PHE A 61 N TRP A 10
SHEET 4 A 6 PHE A 258 ILE A 266 -1 O SER A 263 N TRP A 62
SHEET 5 A 6 TYR A 106 GLU A 111 -1 N TYR A 106 O ALA A 264
SHEET 6 A 6 ALA A 301 VAL A 302 -1 O ALA A 301 N VAL A 110
SHEET 1 B 5 LYS A 34 GLU A 38 0
SHEET 2 B 5 LYS A 6 TRP A 10 1 N ILE A 9 O THR A 36
SHEET 3 B 5 ILE A 59 ALA A 63 1 O PHE A 61 N TRP A 10
SHEET 4 B 5 PHE A 258 ILE A 266 -1 O SER A 263 N TRP A 62
SHEET 5 B 5 GLU A 328 ILE A 329 1 O GLU A 328 N VAL A 259
SHEET 1 C 2 ARG A 98 TYR A 99 0
SHEET 2 C 2 LYS A 102 LEU A 103 -1 O LYS A 102 N TYR A 99
SHEET 1 D 4 SER A 145 LEU A 147 0
SHEET 2 D 4 THR A 222 ASN A 227 1 O ALA A 223 N SER A 145
SHEET 3 D 4 SER A 114 ASN A 118 -1 N ILE A 116 O THR A 225
SHEET 4 D 4 TYR A 242 THR A 245 -1 O THR A 245 N LEU A 115
SHEET 1 E 2 TYR A 167 PHE A 169 0
SHEET 2 E 2 VAL A 181 GLY A 182 -1 O GLY A 182 N TYR A 167
CRYST1 44.540 70.350 58.190 90.00 101.20 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 0.022452 0.000000 0.004446 0.00000
SCALE2 0.000000 0.014215 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017519 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
