HEADER OXIDOREDUCTASE 28-JUL-00 1GC9
TITLE THE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 3-ISOPROPYLMALATE
TITLE 2 DEHYDROGENASE MUTATED AT 172TH FROM ALA TO GLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-ISOPROPYLMALATE DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.85;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: LEUB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: JA221
KEYWDS IPMDH, IMDH, THERMOSTABILITY, DEHYDROGENATION, DECARBOXYLATION,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.QU,S.AKANUMA,N.TANAKA,H.MORIYAMA,T.OSHIMA
REVDAT 8 27-DEC-23 1GC9 1 REMARK
REVDAT 7 10-NOV-21 1GC9 1 SEQADV
REVDAT 6 04-OCT-17 1GC9 1 REMARK
REVDAT 5 13-JUL-11 1GC9 1 VERSN
REVDAT 4 24-FEB-09 1GC9 1 VERSN
REVDAT 3 28-JAN-03 1GC9 1 REMARK
REVDAT 2 01-FEB-01 1GC9 1 JRNL
REVDAT 1 27-SEP-00 1GC9 0
JRNL AUTH C.QU,S.AKANUMA,N.TANAKA,H.MORIYAMA,T.OSHIMA
JRNL TITL DESIGN, X-RAY CRYSTALLOGRAPHY, MOLECULAR MODELLING AND
JRNL TITL 2 THERMAL STABILITY STUDIES OF MUTANT ENZYMES AT SITE 172 OF
JRNL TITL 3 3-ISOPROPYLMALATE DEHYDROGENASE FROM THERMUS THERMOPHILUS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 57 225 2001
JRNL REFN ISSN 0907-4449
JRNL PMID 11173468
JRNL DOI 10.1107/S0907444900017388
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2474507.120
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 16105
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) : 0.173
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1600
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 41.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1474
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 174
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.023
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.340
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) : 2.540 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.760 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 22.270; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 19.210; 2.500
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.PARAM
REMARK 3 TOPOLOGY FILE 4 : PROTEIN.LINK
REMARK 3 TOPOLOGY FILE 5 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GC9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000005031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 7.6
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) : 1.5418
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 : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06400
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONUIM SULFATE, POTASSIUM PHOSPHATE,
REMARK 280 PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 105.37333
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 52.68667
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 52.68667
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 105.37333
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED BY CHAIN A
REMARK 300 AND A SYMETRY PARTNER GENERATED BY THE TWO-FOLD AXIS.
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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 158.06000
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 283 N - CA - C ANGL. DEV. = -15.3 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 127 77.83 -159.80
REMARK 500 ARG A 176 -118.04 -120.36
REMARK 500 VAL A 188 -36.02 -140.22
REMARK 500 SER A 226 58.68 -149.40
REMARK 500 ASP A 231 -86.47 -120.93
REMARK 500 ASN A 237 -70.42 -62.54
REMARK 500 SER A 253 116.20 -166.82
REMARK 500 ALA A 276 58.60 38.65
REMARK 500 ILE A 284 -15.46 40.09
REMARK 500 LEU A 344 46.08 -97.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IPD RELATED DB: PDB
REMARK 900 1IPD CONTAINS THE WILD TYPE ENZYME PRODUCED BY THERMUS THERMOPHILUS.
REMARK 900 RELATED ID: 1OSJ RELATED DB: PDB
REMARK 900 1OSJ CONTAINS A172L.
REMARK 900 RELATED ID: 1GC8 RELATED DB: PDB
REMARK 900 1GC8 CONTAINS A172F.
REMARK 900 RELATED ID: 1DPZ RELATED DB: PDB
REMARK 900 1DPZ CONTAINS THE C-TERMINAL MUTANT OF A172L.
REMARK 900 RELATED ID: 1DR0 RELATED DB: PDB
REMARK 900 1DR0 CONTAINS THE C-TERMINAL MUTANT OF A172L.
REMARK 900 RELATED ID: 1DR8 RELATED DB: PDB
REMARK 900 1DR8 CONTAINS THE C-TERMINAL MUTANT OF A172L.
DBREF 1GC9 A 1 345 UNP Q5SIY4 Q5SIY4_THET8 1 345
SEQADV 1GC9 ARG A 85 UNP Q5SIY4 SER 85 SEE REMARK 999
SEQADV 1GC9 GLY A 172 UNP Q5SIY4 ALA 172 ENGINEERED MUTATION
SEQRES 1 A 345 MET LYS VAL ALA VAL LEU PRO GLY ASP GLY ILE GLY PRO
SEQRES 2 A 345 GLU VAL THR GLU ALA ALA LEU LYS VAL LEU ARG ALA LEU
SEQRES 3 A 345 ASP GLU ALA GLU GLY LEU GLY LEU ALA TYR GLU VAL PHE
SEQRES 4 A 345 PRO PHE GLY GLY ALA ALA ILE ASP ALA PHE GLY GLU PRO
SEQRES 5 A 345 PHE PRO GLU PRO THR ARG LYS GLY VAL GLU GLU ALA GLU
SEQRES 6 A 345 ALA VAL LEU LEU GLY SER VAL GLY GLY PRO LYS TRP ASP
SEQRES 7 A 345 GLY LEU PRO ARG LYS ILE ARG PRO GLU THR GLY LEU LEU
SEQRES 8 A 345 SER LEU ARG LYS SER GLN ASP LEU PHE ALA ASN LEU ARG
SEQRES 9 A 345 PRO ALA LYS VAL PHE PRO GLY LEU GLU ARG LEU SER PRO
SEQRES 10 A 345 LEU LYS GLU GLU ILE ALA ARG GLY VAL ASP VAL LEU ILE
SEQRES 11 A 345 VAL ARG GLU LEU THR GLY GLY ILE TYR PHE GLY GLU PRO
SEQRES 12 A 345 ARG GLY MET SER GLU ALA GLU ALA TRP ASN THR GLU ARG
SEQRES 13 A 345 TYR SER LYS PRO GLU VAL GLU ARG VAL ALA ARG VAL ALA
SEQRES 14 A 345 PHE GLU GLY ALA ARG LYS ARG ARG LYS HIS VAL VAL SER
SEQRES 15 A 345 VAL ASP LYS ALA ASN VAL LEU GLU VAL GLY GLU PHE TRP
SEQRES 16 A 345 ARG LYS THR VAL GLU GLU VAL GLY ARG GLY TYR PRO ASP
SEQRES 17 A 345 VAL ALA LEU GLU HIS GLN TYR VAL ASP ALA MET ALA MET
SEQRES 18 A 345 HIS LEU VAL ARG SER PRO ALA ARG PHE ASP VAL VAL VAL
SEQRES 19 A 345 THR GLY ASN ILE PHE GLY ASP ILE LEU SER ASP LEU ALA
SEQRES 20 A 345 SER VAL LEU PRO GLY SER LEU GLY LEU LEU PRO SER ALA
SEQRES 21 A 345 SER LEU GLY ARG GLY THR PRO VAL PHE GLU PRO VAL HIS
SEQRES 22 A 345 GLY SER ALA PRO ASP ILE ALA GLY LYS GLY ILE ALA ASN
SEQRES 23 A 345 PRO THR ALA ALA ILE LEU SER ALA ALA MET MET LEU GLU
SEQRES 24 A 345 HIS ALA PHE GLY LEU VAL GLU LEU ALA ARG LYS VAL GLU
SEQRES 25 A 345 ASP ALA VAL ALA LYS ALA LEU LEU GLU THR PRO PRO PRO
SEQRES 26 A 345 ASP LEU GLY GLY SER ALA GLY THR GLU ALA PHE THR ALA
SEQRES 27 A 345 THR VAL LEU ARG HIS LEU ALA
FORMUL 2 HOH *55(H2 O)
HELIX 1 1 ILE A 11 GLY A 31 1 21
HELIX 2 2 GLY A 42 GLY A 50 1 9
HELIX 3 3 PRO A 54 ALA A 64 1 11
HELIX 4 4 GLY A 74 GLY A 79 1 6
HELIX 5 5 PRO A 81 ILE A 84 5 4
HELIX 6 6 ARG A 85 GLN A 97 1 13
HELIX 7 7 LEU A 112 SER A 116 5 5
HELIX 8 8 LYS A 119 ARG A 124 1 6
HELIX 9 9 SER A 158 LYS A 175 1 18
HELIX 10 10 LEU A 189 ARG A 204 1 16
HELIX 11 11 VAL A 216 SER A 226 1 11
HELIX 12 12 PRO A 227 PHE A 230 5 4
HELIX 13 13 GLY A 236 LEU A 250 1 15
HELIX 14 14 SER A 253 LEU A 256 5 4
HELIX 15 15 ALA A 276 ALA A 280 5 5
HELIX 16 16 PRO A 287 PHE A 302 1 16
HELIX 17 17 LEU A 304 THR A 322 1 19
HELIX 18 18 PRO A 324 GLY A 328 5 5
HELIX 19 19 GLY A 332 HIS A 343 1 12
SHEET 1 A10 ALA A 35 VAL A 38 0
SHEET 2 A10 LYS A 2 GLY A 8 1 N VAL A 3 O ALA A 35
SHEET 3 A10 ALA A 66 SER A 71 1 O ALA A 66 N ALA A 4
SHEET 4 A10 VAL A 268 PRO A 271 1 O PHE A 269 N LEU A 69
SHEET 5 A10 PRO A 258 GLY A 263 -1 O SER A 259 N GLU A 270
SHEET 6 A10 LEU A 99 LYS A 107 -1 N PHE A 100 O LEU A 262
SHEET 7 A10 ASP A 127 GLU A 133 -1 O VAL A 128 N ALA A 106
SHEET 8 A10 VAL A 232 THR A 235 1 O VAL A 233 N VAL A 131
SHEET 9 A10 HIS A 179 ASP A 184 1 O HIS A 179 N VAL A 232
SHEET 10 A10 ALA A 210 TYR A 215 1 O ALA A 210 N VAL A 180
SHEET 1 B 2 GLY A 145 MET A 146 0
SHEET 2 B 2 ALA A 151 TRP A 152 -1 O TRP A 152 N GLY A 145
CISPEP 1 GLU A 142 PRO A 143 0 0.12
CRYST1 78.610 78.610 158.060 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 0.012721 0.007344 0.000000 0.00000
SCALE2 0.000000 0.014689 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
