HEADER LYASE 25-FEB-02 1L2U
TITLE OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OMP DECARBOXYLASE, OMPDCASE;
COMPND 5 EC: 4.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLFF8
KEYWDS BETA-ALPHA-BARREL, HOMODIMER, TWINNED CRYSTALS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.HARRIS,J.C.POULSEN,K.F.JENSEN,S.LARSEN
REVDAT 5 16-AUG-23 1L2U 1 REMARK
REVDAT 4 07-MAR-18 1L2U 1 REMARK
REVDAT 3 24-FEB-09 1L2U 1 VERSN
REVDAT 2 16-OCT-02 1L2U 1 AUTHOR JRNL
REVDAT 1 13-MAR-02 1L2U 0
JRNL AUTH P.HARRIS,J.C.POULSEN,K.F.JENSEN,S.LARSEN
JRNL TITL SUBSTRATE BINDING INDUCES DOMAIN MOVEMENTS IN OROTIDINE
JRNL TITL 2 5'-MONOPHOSPHATE DECARBOXYLASE
JRNL REF J.MOL.BIOL. V. 18 1019 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12054799
JRNL DOI 10.1016/S0022-2836(02)00200-0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.HARRIS,J.C.NAVARRO POULSEN,K.F.JENSEN,S.LARSEN
REMARK 1 TITL STRUCTURAL BASIS FOR THE CATALYTIC MECHANISM OF A PROFICIENT
REMARK 1 TITL 2 ENZYME: OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE
REMARK 1 REF BIOCHEMISTRY V. 39 4217 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI992952R
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.C.POULSEN,P.HARRIS,K.F.JENSEN,S.LARSEN
REMARK 1 TITL SELENOMETHIONINE SUBSTITUTION OF OROTIDINE-5'-MONOPHOSPHATE
REMARK 1 TITL 2 DECARBOXYLASE CAUSES A CHANGE IN CRYSTAL CONTACTS AND SPACE
REMARK 1 TITL 3 GROUP
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 57 1251 2001
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444901010393
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : IN SHELLS
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.162
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.159
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2032
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 39834
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 ANGLE DISTANCES (A) : 0.025
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.060
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.032
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.028
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 99.9
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0159
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42389
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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 1EIX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, SODIUM ACETATE, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 70.24667
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 35.12333
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 35.12333
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 70.24667
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
REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B1111 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 THR A 2
REMARK 465 LEU A 3
REMARK 465 THR A 4
REMARK 465 ALA A 5
REMARK 465 SER A 6
REMARK 465 SER A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 ARG A 10
REMARK 465 GLY A 195
REMARK 465 SER A 196
REMARK 465 GLU A 197
REMARK 465 ALA A 198
REMARK 465 GLY A 199
REMARK 465 ASP A 200
REMARK 465 GLN A 201
REMARK 465 ARG A 202
REMARK 465 ARG A 203
REMARK 465 SER A 244
REMARK 465 ALA A 245
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 LEU B 3
REMARK 465 THR B 4
REMARK 465 ALA B 5
REMARK 465 SER B 6
REMARK 465 SER B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 ARG B 10
REMARK 465 ALA B 11
REMARK 465 GLY B 195
REMARK 465 SER B 196
REMARK 465 GLU B 197
REMARK 465 ALA B 198
REMARK 465 GLY B 199
REMARK 465 ASP B 200
REMARK 465 GLN B 201
REMARK 465 ARG B 202
REMARK 465 ARG B 203
REMARK 465 SER B 244
REMARK 465 ALA B 245
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 ARG A 42 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PHE A 69 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG B 64 NE - CZ - NH1 ANGL. DEV. = 3.6 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 VAL A 12 140.51 -29.89
REMARK 500 GLU A 48 -77.74 -57.52
REMARK 500 LYS A 73 66.72 32.26
REMARK 500 THR A 128 -96.78 -102.59
REMARK 500 MET A 205 173.98 -56.41
REMARK 500 GLN A 226 33.08 -91.87
REMARK 500 ASP A 229 60.87 68.09
REMARK 500 LYS B 73 58.36 33.17
REMARK 500 THR B 128 -92.29 -104.19
REMARK 500 ASP B 229 67.77 65.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EIX RELATED DB: PDB
REMARK 900 1EIX CONTAINS THE SAME PROTEIN COMPLEXED WITH BMP
REMARK 900 RELATED ID: 1JJK RELATED DB: PDB
REMARK 900 1JJK CONTAINS THE SEMET SUBSTITUTED FORM OF THE SAME PROTEIN
REMARK 900 COMPLEXED WITH BMP
DBREF 1L2U A 1 245 UNP P08244 PYRF_ECOLI 1 245
DBREF 1L2U B 1 245 UNP P08244 PYRF_ECOLI 1 245
SEQRES 1 A 245 MET THR LEU THR ALA SER SER SER SER ARG ALA VAL THR
SEQRES 2 A 245 ASN SER PRO VAL VAL VAL ALA LEU ASP TYR HIS ASN ARG
SEQRES 3 A 245 ASP ASP ALA LEU ALA PHE VAL ASP LYS ILE ASP PRO ARG
SEQRES 4 A 245 ASP CYS ARG LEU LYS VAL GLY LYS GLU MET PHE THR LEU
SEQRES 5 A 245 PHE GLY PRO GLN PHE VAL ARG GLU LEU GLN GLN ARG GLY
SEQRES 6 A 245 PHE ASP ILE PHE LEU ASP LEU LYS PHE HIS ASP ILE PRO
SEQRES 7 A 245 ASN THR ALA ALA HIS ALA VAL ALA ALA ALA ALA ASP LEU
SEQRES 8 A 245 GLY VAL TRP MET VAL ASN VAL HIS ALA SER GLY GLY ALA
SEQRES 9 A 245 ARG MET MET THR ALA ALA ARG GLU ALA LEU VAL PRO PHE
SEQRES 10 A 245 GLY LYS ASP ALA PRO LEU LEU ILE ALA VAL THR VAL LEU
SEQRES 11 A 245 THR SER MET GLU ALA SER ASP LEU VAL ASP LEU GLY MET
SEQRES 12 A 245 THR LEU SER PRO ALA ASP TYR ALA GLU ARG LEU ALA ALA
SEQRES 13 A 245 LEU THR GLN LYS CYS GLY LEU ASP GLY VAL VAL CYS SER
SEQRES 14 A 245 ALA GLN GLU ALA VAL ARG PHE LYS GLN VAL PHE GLY GLN
SEQRES 15 A 245 GLU PHE LYS LEU VAL THR PRO GLY ILE ARG PRO GLN GLY
SEQRES 16 A 245 SER GLU ALA GLY ASP GLN ARG ARG ILE MET THR PRO GLU
SEQRES 17 A 245 GLN ALA LEU SER ALA GLY VAL ASP TYR MET VAL ILE GLY
SEQRES 18 A 245 ARG PRO VAL THR GLN SER VAL ASP PRO ALA GLN THR LEU
SEQRES 19 A 245 LYS ALA ILE ASN ALA SER LEU GLN ARG SER ALA
SEQRES 1 B 245 MET THR LEU THR ALA SER SER SER SER ARG ALA VAL THR
SEQRES 2 B 245 ASN SER PRO VAL VAL VAL ALA LEU ASP TYR HIS ASN ARG
SEQRES 3 B 245 ASP ASP ALA LEU ALA PHE VAL ASP LYS ILE ASP PRO ARG
SEQRES 4 B 245 ASP CYS ARG LEU LYS VAL GLY LYS GLU MET PHE THR LEU
SEQRES 5 B 245 PHE GLY PRO GLN PHE VAL ARG GLU LEU GLN GLN ARG GLY
SEQRES 6 B 245 PHE ASP ILE PHE LEU ASP LEU LYS PHE HIS ASP ILE PRO
SEQRES 7 B 245 ASN THR ALA ALA HIS ALA VAL ALA ALA ALA ALA ASP LEU
SEQRES 8 B 245 GLY VAL TRP MET VAL ASN VAL HIS ALA SER GLY GLY ALA
SEQRES 9 B 245 ARG MET MET THR ALA ALA ARG GLU ALA LEU VAL PRO PHE
SEQRES 10 B 245 GLY LYS ASP ALA PRO LEU LEU ILE ALA VAL THR VAL LEU
SEQRES 11 B 245 THR SER MET GLU ALA SER ASP LEU VAL ASP LEU GLY MET
SEQRES 12 B 245 THR LEU SER PRO ALA ASP TYR ALA GLU ARG LEU ALA ALA
SEQRES 13 B 245 LEU THR GLN LYS CYS GLY LEU ASP GLY VAL VAL CYS SER
SEQRES 14 B 245 ALA GLN GLU ALA VAL ARG PHE LYS GLN VAL PHE GLY GLN
SEQRES 15 B 245 GLU PHE LYS LEU VAL THR PRO GLY ILE ARG PRO GLN GLY
SEQRES 16 B 245 SER GLU ALA GLY ASP GLN ARG ARG ILE MET THR PRO GLU
SEQRES 17 B 245 GLN ALA LEU SER ALA GLY VAL ASP TYR MET VAL ILE GLY
SEQRES 18 B 245 ARG PRO VAL THR GLN SER VAL ASP PRO ALA GLN THR LEU
SEQRES 19 B 245 LYS ALA ILE ASN ALA SER LEU GLN ARG SER ALA
FORMUL 3 HOH *121(H2 O)
HELIX 1 1 ASN A 25 LYS A 35 1 11
HELIX 2 2 GLY A 46 ARG A 64 1 19
HELIX 3 3 ILE A 77 LEU A 91 1 15
HELIX 4 4 GLY A 103 VAL A 115 1 13
HELIX 5 5 PRO A 116 ALA A 121 5 6
HELIX 6 6 GLU A 134 GLY A 142 1 9
HELIX 7 7 SER A 146 GLY A 162 1 17
HELIX 8 8 SER A 169 GLY A 181 1 13
HELIX 9 9 THR A 206 GLY A 214 1 9
HELIX 10 10 GLY A 221 GLN A 226 1 6
HELIX 11 11 ASP A 229 LEU A 241 1 13
HELIX 12 12 ASN B 25 LYS B 35 1 11
HELIX 13 13 GLY B 46 GLY B 54 1 9
HELIX 14 14 GLY B 54 ARG B 64 1 11
HELIX 15 15 ILE B 77 LEU B 91 1 15
HELIX 16 16 GLY B 103 VAL B 115 1 13
HELIX 17 17 PRO B 116 ALA B 121 5 6
HELIX 18 18 GLU B 134 LEU B 141 1 8
HELIX 19 19 SER B 146 GLY B 162 1 17
HELIX 20 20 SER B 169 GLY B 181 1 13
HELIX 21 21 THR B 206 GLY B 214 1 9
HELIX 22 22 GLY B 221 GLN B 226 1 6
HELIX 23 23 ASP B 229 ARG B 243 1 15
SHEET 1 A 9 VAL A 17 LEU A 21 0
SHEET 2 A 9 ARG A 42 VAL A 45 1 O ARG A 42 N VAL A 19
SHEET 3 A 9 ILE A 68 PHE A 74 1 O ASP A 71 N VAL A 45
SHEET 4 A 9 MET A 95 HIS A 99 1 O MET A 95 N LEU A 70
SHEET 5 A 9 LEU A 123 VAL A 127 1 O VAL A 127 N VAL A 98
SHEET 6 A 9 GLY A 165 VAL A 167 1 O VAL A 167 N ALA A 126
SHEET 7 A 9 LYS A 185 PRO A 189 1 O VAL A 187 N VAL A 166
SHEET 8 A 9 TYR A 217 ILE A 220 1 O VAL A 219 N THR A 188
SHEET 9 A 9 VAL A 17 LEU A 21 1 N VAL A 18 O MET A 218
SHEET 1 B 9 VAL B 17 LEU B 21 0
SHEET 2 B 9 ARG B 42 VAL B 45 1 O LYS B 44 N VAL B 19
SHEET 3 B 9 ILE B 68 PHE B 74 1 O PHE B 69 N LEU B 43
SHEET 4 B 9 MET B 95 HIS B 99 1 O HIS B 99 N PHE B 74
SHEET 5 B 9 LEU B 123 VAL B 127 1 O VAL B 127 N VAL B 98
SHEET 6 B 9 GLY B 165 VAL B 167 1 O VAL B 167 N ALA B 126
SHEET 7 B 9 LYS B 185 THR B 188 1 O VAL B 187 N VAL B 166
SHEET 8 B 9 TYR B 217 ILE B 220 1 O VAL B 219 N THR B 188
SHEET 9 B 9 VAL B 17 LEU B 21 1 N VAL B 18 O MET B 218
CRYST1 142.690 142.690 105.370 90.00 90.00 120.00 P 32 2 1 12
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 0.007008 0.004046 0.000000 0.00000
SCALE2 0.000000 0.008092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009490 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
