HEADER ISOMERASE 01-AUG-01 1JPD
TITLE L-ALA-D/L-GLU EPIMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-ALA-D/L-GLU EPIMERASE;
COMPND 3 CHAIN: X;
COMPND 4 EC: 5.5.-.-;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS ENOLASE SUPERFAMILY, MUCONATE LACTONIZING ENZYME SUBGROUP, ALPHA/BETA
KEYWDS 2 BARREL, STRUCTURAL GENOMICS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.GULICK,D.M.Z.SCHMIDT,J.A.GERLT,I.RAYMENT
REVDAT 4 07-FEB-24 1JPD 1 SEQADV
REVDAT 3 24-FEB-09 1JPD 1 VERSN
REVDAT 2 01-APR-03 1JPD 1 JRNL
REVDAT 1 21-DEC-01 1JPD 0
JRNL AUTH A.M.GULICK,D.M.SCHMIDT,J.A.GERLT,I.RAYMENT
JRNL TITL EVOLUTION OF ENZYMATIC ACTIVITIES IN THE ENOLASE
JRNL TITL 2 SUPERFAMILY: CRYSTAL STRUCTURES OF THE L-ALA-D/L-GLU
JRNL TITL 3 EPIMERASES FROM ESCHERICHIA COLI AND BACILLUS SUBTILIS.
JRNL REF BIOCHEMISTRY V. 40 15716 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11747448
JRNL DOI 10.1021/BI011641P
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 20.40
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) (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 17409
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : THROUGHOUT
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 916
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 5.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2726
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 : 2395
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.34
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 113
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 : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.70008
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1000
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 400-500MM NACL, 50 MM SUCCINATE, PH
REMARK 280 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 79.44050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 42.10150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.10150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.72025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.10150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 42.10150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 119.16075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 42.10150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.10150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.72025
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 42.10150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.10150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 119.16075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 79.44050
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: X
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 PHE X 17
REMARK 465 VAL X 18
REMARK 465 ILE X 19
REMARK 465 ALA X 20
REMARK 465 ARG X 21
REMARK 465 GLY X 22
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER X 23 OG
REMARK 470 ARG X 24 CG CD NE CZ NH1 NH2
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 ARG X 24 -79.62 -47.68
REMARK 500 GLU X 36 64.09 -100.27
REMARK 500 GLU X 37 95.35 52.76
REMARK 500 ARG X 50 -6.83 -54.65
REMARK 500 ASP X 153 -149.41 -110.06
REMARK 500 LEU X 156 46.03 35.60
REMARK 500 ASN X 178 55.03 39.36
REMARK 500 GLU X 179 17.46 59.81
REMARK 500 GLN X 203 67.35 31.88
REMARK 500 ASP X 209 59.61 -166.41
REMARK 500 ASP X 225 -80.73 -122.68
REMARK 500 THR X 316 109.65 -42.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2MUC RELATED DB: PDB
REMARK 900 MUCONATE LACTONIZING ENZYME
REMARK 900 RELATED ID: 1FHV RELATED DB: PDB
REMARK 900 O-SUCCINYLBENZOATE SYNTASE
DBREF 1JPD X 1 321 UNP P51981 YCJG_ECOLI 15 335
SEQADV 1JPD GLY X -2 UNP P51981 INSERTION
SEQADV 1JPD SER X -1 UNP P51981 INSERTION
SEQADV 1JPD HIS X 0 UNP P51981 INSERTION
SEQRES 1 X 324 GLY SER HIS MET ARG THR VAL LYS VAL PHE GLU GLU ALA
SEQRES 2 X 324 TRP PRO LEU HIS THR PRO PHE VAL ILE ALA ARG GLY SER
SEQRES 3 X 324 ARG SER GLU ALA ARG VAL VAL VAL VAL GLU LEU GLU GLU
SEQRES 4 X 324 GLU GLY ILE LYS GLY THR GLY GLU CYS THR PRO TYR PRO
SEQRES 5 X 324 ARG TYR GLY GLU SER ASP ALA SER VAL MET ALA GLN ILE
SEQRES 6 X 324 MET SER VAL VAL PRO GLN LEU GLU LYS GLY LEU THR ARG
SEQRES 7 X 324 GLU GLU LEU GLN LYS ILE LEU PRO ALA GLY ALA ALA ARG
SEQRES 8 X 324 ASN ALA LEU ASP CYS ALA LEU TRP ASP LEU ALA ALA ARG
SEQRES 9 X 324 ARG GLN GLN GLN SER LEU ALA ASP LEU ILE GLY ILE THR
SEQRES 10 X 324 LEU PRO GLU THR VAL ILE THR ALA GLN THR VAL VAL ILE
SEQRES 11 X 324 GLY THR PRO ASP GLN MET ALA ASN SER ALA SER THR LEU
SEQRES 12 X 324 TRP GLN ALA GLY ALA LYS LEU LEU LYS VAL LYS LEU ASP
SEQRES 13 X 324 ASN HIS LEU ILE SER GLU ARG MET VAL ALA ILE ARG THR
SEQRES 14 X 324 ALA VAL PRO ASP ALA THR LEU ILE VAL ASP ALA ASN GLU
SEQRES 15 X 324 SER TRP ARG ALA GLU GLY LEU ALA ALA ARG CYS GLN LEU
SEQRES 16 X 324 LEU ALA ASP LEU GLY VAL ALA MET LEU GLU GLN PRO LEU
SEQRES 17 X 324 PRO ALA GLN ASP ASP ALA ALA LEU GLU ASN PHE ILE HIS
SEQRES 18 X 324 PRO LEU PRO ILE CYS ALA ASP GLU SER CYS HIS THR ARG
SEQRES 19 X 324 SER ASN LEU LYS ALA LEU LYS GLY ARG TYR GLU MET VAL
SEQRES 20 X 324 ASN ILE LYS LEU ASP LYS THR GLY GLY LEU THR GLU ALA
SEQRES 21 X 324 LEU ALA LEU ALA THR GLU ALA ARG ALA GLN GLY PHE SER
SEQRES 22 X 324 LEU MET LEU GLY CYS MET LEU CYS THR SER ARG ALA ILE
SEQRES 23 X 324 SER ALA ALA LEU PRO LEU VAL PRO GLN VAL SER PHE ALA
SEQRES 24 X 324 ASP LEU ASP GLY PRO THR TRP LEU ALA VAL ASP VAL GLU
SEQRES 25 X 324 PRO ALA LEU GLN PHE THR THR GLY GLU LEU HIS LEU
FORMUL 2 HOH *144(H2 O)
HELIX 1 1 TYR X 48 GLY X 52 5 5
HELIX 2 2 SER X 54 SER X 64 1 11
HELIX 3 3 VAL X 65 LYS X 71 1 7
HELIX 4 4 THR X 74 LEU X 82 1 9
HELIX 5 5 GLY X 85 ARG X 102 1 18
HELIX 6 6 SER X 106 GLY X 112 1 7
HELIX 7 7 THR X 129 ALA X 143 1 15
HELIX 8 8 LEU X 156 VAL X 168 1 13
HELIX 9 9 GLY X 185 LEU X 196 1 12
HELIX 10 10 ASP X 210 ASN X 215 5 6
HELIX 11 11 THR X 230 SER X 232 5 3
HELIX 12 12 ASN X 233 LYS X 238 1 6
HELIX 13 13 LYS X 247 GLY X 252 1 6
HELIX 14 14 GLY X 253 GLN X 267 1 15
HELIX 15 15 THR X 279 LEU X 287 1 9
HELIX 16 16 PRO X 288 VAL X 293 5 6
HELIX 17 17 ASP X 299 LEU X 304 5 6
SHEET 1 A 3 THR X 3 PRO X 12 0
SHEET 2 A 3 GLU X 26 GLU X 36 -1 O VAL X 31 N PHE X 7
SHEET 3 A 3 ILE X 39 CYS X 45 -1 O GLY X 41 N LEU X 34
SHEET 1 B 3 THR X 118 ILE X 120 0
SHEET 2 B 3 GLU X 318 HIS X 320 -1 O LEU X 319 N VAL X 119
SHEET 3 B 3 GLN X 313 THR X 315 -1 N THR X 315 O GLU X 318
SHEET 1 C 8 GLN X 123 VAL X 125 0
SHEET 2 C 8 LEU X 147 LYS X 151 1 O LYS X 149 N GLN X 123
SHEET 3 C 8 THR X 172 ASP X 176 1 O ILE X 174 N VAL X 150
SHEET 4 C 8 MET X 200 GLU X 202 1 O GLU X 202 N VAL X 175
SHEET 5 C 8 ILE X 222 ALA X 224 1 O CYS X 223 N LEU X 201
SHEET 6 C 8 MET X 243 ILE X 246 1 O ASN X 245 N ALA X 224
SHEET 7 C 8 SER X 270 LEU X 273 1 O MET X 272 N ILE X 246
SHEET 8 C 8 PHE X 295 ALA X 296 1 O PHE X 295 N LEU X 273
CISPEP 1 GLU X 309 PRO X 310 0 0.35
CRYST1 84.203 84.203 158.881 90.00 90.00 90.00 P 41 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 0.011876 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011876 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006294 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
