HEADER OXIDOREDUCTASE 19-MAY-95 1IDM
TITLE 3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IPMDH;
COMPND 5 EC: 1.1.1.85;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JA221;
SOURCE 8 OTHER_DETAILS: HYBRID BETWEEN THERMUS IPMDH (332 RESIDUES) AND YEAST
SOURCE 9 IPMDH (11 RESIDUES)
KEYWDS CHIMERA, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SAKURAI,M.OHZEKI,H.MORIYAMA,M.SATO,N.TANAKA
REVDAT 4 07-FEB-24 1IDM 1 SEQADV
REVDAT 3 13-JUL-11 1IDM 1 VERSN
REVDAT 2 24-FEB-09 1IDM 1 VERSN
REVDAT 1 15-SEP-95 1IDM 0
JRNL AUTH M.SAKURAI,M.OHZEKI,K.MIYAZAKI,H.MORIYAMA,M.SATO,N.TANAKA,
JRNL AUTH 2 T.OSHIMA
JRNL TITL STRUCTURE OF A LOOP-DELETED VARIANT OF 3-ISOPROPYLMALATE
JRNL TITL 2 DEHYDROGENASE FROM THERMUS THERMOPHILUS: AN INTERNAL
JRNL TITL 3 REPRIEVE TOLERANCE MECHANISM.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 52 124 1996
JRNL REFN ISSN 0907-4449
JRNL PMID 15299733
JRNL DOI 10.1107/S0907444995007190
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.YAMADA,N.AKUTSU,K.MIYAZAKI,K.KAKINUMA,M.YOSHIDA,T.OSHIMA
REMARK 1 TITL PURIFICATION, CATALYTIC PROPERTIES AND THERMAL STABILITY OF
REMARK 1 TITL 2 THREO-DS-3-ISOPROPYLMALATE DEHYDROGENASE CODED BY LEUB GENE
REMARK 1 TITL 3 FROM AN EXTREME THERMOPHILE, THERMUS THERMOPHILUS STRAIN HB8
REMARK 1 REF J.BIOCHEM.(TOKYO) V. 108 449 1990
REMARK 1 REFN ISSN 0021-924X
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 76.0
REMARK 3 NUMBER OF REFLECTIONS : 20014
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 109
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.76
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.344
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 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 1IDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174114.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-94
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROCESS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27190
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03800
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.38000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.69000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.69000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.38000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24930 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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 158.07000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 281 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 125 75.64 -160.16
REMARK 500 ARG A 174 -117.58 -115.76
REMARK 500 SER A 224 64.37 -151.11
REMARK 500 ASP A 229 -85.64 -125.09
REMARK 500 SER A 251 100.34 -167.65
REMARK 500 ALA A 274 61.02 34.59
REMARK 500 ILE A 282 -27.37 43.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IDM A 1 343 UNP P00351 LEU3_THETH 1 345
SEQADV 1IDM GLY A 78 UNP P00351 INSERTION
SEQADV 1IDM THR A 79 UNP P00351 ASP 78 CONFLICT
SEQADV 1IDM SER A 81 UNP P00351 LEU 80 CONFLICT
SEQADV 1IDM VAL A 82 UNP P00351 PRO 81 CONFLICT
SEQADV 1IDM A UNP P00351 LYS 83 DELETION
SEQADV 1IDM A UNP P00351 ILE 84 DELETION
SEQADV 1IDM A UNP P00351 SER 85 DELETION
SEQADV 1IDM GLN A 86 UNP P00351 THR 88 CONFLICT
SEQRES 1 A 343 MET LYS VAL ALA VAL LEU PRO GLY ASP GLY ILE GLY PRO
SEQRES 2 A 343 GLU VAL THR GLU ALA ALA LEU LYS VAL LEU ARG ALA LEU
SEQRES 3 A 343 ASP GLU ALA GLU GLY LEU GLY LEU ALA TYR GLU VAL PHE
SEQRES 4 A 343 PRO PHE GLY GLY ALA ALA ILE ASP ALA PHE GLY GLU PRO
SEQRES 5 A 343 PHE PRO GLU PRO THR ARG LYS GLY VAL GLU GLU ALA GLU
SEQRES 6 A 343 ALA VAL LEU LEU GLY SER VAL GLY GLY PRO LYS TRP GLY
SEQRES 7 A 343 THR GLY SER VAL ARG PRO GLU GLN GLY LEU LEU SER LEU
SEQRES 8 A 343 ARG LYS SER GLN ASP LEU PHE ALA ASN LEU ARG PRO ALA
SEQRES 9 A 343 LYS VAL PHE PRO GLY LEU GLU ARG LEU SER PRO LEU LYS
SEQRES 10 A 343 GLU GLU ILE ALA ARG GLY VAL ASP VAL LEU ILE VAL ARG
SEQRES 11 A 343 GLU LEU THR GLY GLY ILE TYR PHE GLY GLU PRO ARG GLY
SEQRES 12 A 343 MET SER GLU ALA GLU ALA TRP ASN THR GLU ARG TYR SER
SEQRES 13 A 343 LYS PRO GLU VAL GLU ARG VAL ALA ARG VAL ALA PHE GLU
SEQRES 14 A 343 ALA ALA ARG LYS ARG ARG LYS HIS VAL VAL SER VAL ASP
SEQRES 15 A 343 LYS ALA ASN VAL LEU GLU VAL GLY GLU PHE TRP ARG LYS
SEQRES 16 A 343 THR VAL GLU GLU VAL GLY ARG GLY TYR PRO ASP VAL ALA
SEQRES 17 A 343 LEU GLU HIS GLN TYR VAL ASP ALA MET ALA MET HIS LEU
SEQRES 18 A 343 VAL ARG SER PRO ALA ARG PHE ASP VAL VAL VAL THR GLY
SEQRES 19 A 343 ASN ILE PHE GLY ASP ILE LEU SER ASP LEU ALA SER VAL
SEQRES 20 A 343 LEU PRO GLY SER LEU GLY LEU LEU PRO SER ALA SER LEU
SEQRES 21 A 343 GLY ARG GLY THR PRO VAL PHE GLU PRO VAL HIS GLY SER
SEQRES 22 A 343 ALA PRO ASP ILE ALA GLY LYS GLY ILE ALA ASN PRO THR
SEQRES 23 A 343 ALA ALA ILE LEU SER ALA ALA MET MET LEU GLU HIS ALA
SEQRES 24 A 343 PHE GLY LEU VAL GLU LEU ALA ARG LYS VAL GLU ASP ALA
SEQRES 25 A 343 VAL ALA LYS ALA LEU LEU GLU THR PRO PRO PRO ASP LEU
SEQRES 26 A 343 GLY GLY SER ALA GLY THR GLU ALA PHE THR ALA THR VAL
SEQRES 27 A 343 LEU ARG HIS LEU ALA
FORMUL 2 HOH *109(H2 O)
HELIX 1 1 GLY A 12 GLU A 30 1 19
HELIX 2 2 GLY A 43 PHE A 49 1 7
HELIX 3 3 GLU A 55 GLU A 63 1 9
HELIX 4 4 PRO A 75 TRP A 77 5 3
HELIX 5 5 PRO A 84 SER A 94 5 11
HELIX 6 6 GLU A 111 LEU A 113 5 3
HELIX 7 7 GLU A 118 ALA A 121 1 4
HELIX 8 8 LYS A 157 LYS A 173 1 17
HELIX 9 9 GLU A 188 GLY A 203 1 16
HELIX 10 10 VAL A 214 ARG A 223 1 10
HELIX 11 11 PRO A 225 ARG A 227 5 3
HELIX 12 12 ASN A 235 LEU A 248 1 14
HELIX 13 13 LEU A 252 LEU A 254 5 3
HELIX 14 14 THR A 286 HIS A 298 1 13
HELIX 15 15 VAL A 303 GLU A 319 1 17
HELIX 16 16 PRO A 323 LEU A 325 5 3
HELIX 17 17 THR A 331 HIS A 341 1 11
SHEET 1 A10 ALA A 35 VAL A 38 0
SHEET 2 A10 LYS A 2 LEU A 6 1 N VAL A 3 O ALA A 35
SHEET 3 A10 ALA A 66 LEU A 69 1 N ALA A 66 O ALA A 4
SHEET 4 A10 PRO A 265 PRO A 269 1 N PRO A 265 O VAL A 67
SHEET 5 A10 PRO A 256 GLY A 261 -1 N SER A 259 O VAL A 266
SHEET 6 A10 LEU A 97 LYS A 105 -1 N LEU A 101 O ALA A 258
SHEET 7 A10 ASP A 125 GLU A 131 -1 N ARG A 130 O ASN A 100
SHEET 8 A10 VAL A 230 THR A 233 1 N VAL A 231 O LEU A 127
SHEET 9 A10 HIS A 177 ASP A 182 1 N VAL A 179 O VAL A 230
SHEET 10 A10 ALA A 208 TYR A 213 1 N ALA A 208 O VAL A 178
CISPEP 1 GLU A 140 PRO A 141 0 -1.21
CRYST1 78.450 78.450 158.070 90.00 90.00 120.00 P 32 2 1 6
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 0.012747 0.007359 0.000000 0.00000
SCALE2 0.000000 0.014719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006326 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
