HEADER LYASE 26-SEP-14 4WIL
TITLE CRYSTAL STRUCTURE OF DCOH2 S51T
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 34-136;
COMPND 5 SYNONYM: PHS 2,4-ALPHA-HYDROXY-TETRAHYDROPTERIN DEHYDRATASE 2,DCOH-
COMPND 6 LIKE PROTEIN DCOHM,DIMERIZATION COFACTOR OF HEPATOCYTE NUCLEAR FACTOR
COMPND 7 1 FROM MUSCLE,HNF-1-ALPHA DIMERIZATION COFACTOR;
COMPND 8 EC: 4.2.1.96;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PCBD2, DCOH2, DCOHM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS BIFUNCTIONAL, KINETIC STABILITY, COACTIVATOR, TETRAHYDROBIOPTERIN
KEYWDS 2 RECYCLING, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.WANG,R.B.ROSE
REVDAT 7 27-SEP-23 4WIL 1 REMARK
REVDAT 6 27-NOV-19 4WIL 1 REMARK
REVDAT 5 27-SEP-17 4WIL 1 REMARK
REVDAT 4 06-SEP-17 4WIL 1 SOURCE JRNL REMARK
REVDAT 3 25-FEB-15 4WIL 1 JRNL
REVDAT 2 14-JAN-15 4WIL 1 JRNL
REVDAT 1 31-DEC-14 4WIL 0
JRNL AUTH D.WANG,M.W.COCO,R.B.ROSE
JRNL TITL INTERACTIONS WITH THE BIFUNCTIONAL INTERFACE OF THE
JRNL TITL 2 TRANSCRIPTIONAL COACTIVATOR DCOH1 ARE KINETICALLY REGULATED.
JRNL REF J.BIOL.CHEM. V. 290 4319 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 25538247
JRNL DOI 10.1074/JBC.M114.616870
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 45081
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2291
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 25.0016 - 3.4168 0.95 2939 158 0.1759 0.1872
REMARK 3 2 3.4168 - 2.7131 0.99 2956 168 0.1686 0.1729
REMARK 3 3 2.7131 - 2.3704 0.99 2904 140 0.1677 0.1697
REMARK 3 4 2.3704 - 2.1538 0.98 2837 153 0.1404 0.1685
REMARK 3 5 2.1538 - 1.9995 0.97 2797 152 0.1421 0.1562
REMARK 3 6 1.9995 - 1.8817 0.96 2734 180 0.1376 0.1609
REMARK 3 7 1.8817 - 1.7875 0.95 2742 138 0.1248 0.1440
REMARK 3 8 1.7875 - 1.7097 0.95 2750 153 0.1099 0.1622
REMARK 3 9 1.7097 - 1.6439 0.94 2705 134 0.1043 0.1361
REMARK 3 10 1.6439 - 1.5872 0.94 2712 135 0.1020 0.1243
REMARK 3 11 1.5872 - 1.5375 0.93 2647 145 0.1127 0.1668
REMARK 3 12 1.5375 - 1.4936 0.88 2526 116 0.1488 0.1591
REMARK 3 13 1.4936 - 1.4543 0.86 2445 141 0.1697 0.1959
REMARK 3 14 1.4543 - 1.4188 0.85 2441 142 0.2128 0.2305
REMARK 3 15 1.4188 - 1.3866 0.87 2468 116 0.2694 0.2793
REMARK 3 16 1.3866 - 1.3570 0.76 2187 120 0.3909 0.4604
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 60.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.50140
REMARK 3 B22 (A**2) : 1.50140
REMARK 3 B33 (A**2) : -3.00270
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1591
REMARK 3 ANGLE : 1.045 2153
REMARK 3 CHIRALITY : 0.078 231
REMARK 3 PLANARITY : 0.005 278
REMARK 3 DIHEDRAL : 12.270 553
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203735.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : FOCUSSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48837
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.360
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 58.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 0.95300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.980
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1RU0
REMARK 200
REMARK 200 REMARK: HEXAGONAL PYRAMIDS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 8% PEG 8,000 MIXING 0.5 UL
REMARK 280 PROTEIN AND 1 UL RESERVOIR, PH 7.5, EVAPORATION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 38.35467
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 76.70933
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 76.70933
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 38.35467
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 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 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 A 232 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 233 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 224 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 SER B 102
REMARK 465 LEU B 103
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 ASP A 4 CB CG OD1 OD2
REMARK 470 GLN A 6 CG CD OE1 NE2
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 ASP A 14 CG OD1 OD2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 LYS A 98 CG CD CE NZ
REMARK 470 LEU A 103 CG CD1 CD2
REMARK 470 ASP B 4 CB CG OD1 OD2
REMARK 470 GLN B 6 CG CD OE1 NE2
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 HIS B 80 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 201 O HOH B 201 4545 2.15
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 TYR A 70 -111.42 52.86
REMARK 500 TYR B 70 -111.54 53.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 278 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B 284 DISTANCE = 6.09 ANGSTROMS
DBREF 4WIL A 1 103 UNP Q9CZL5 PHS2_MOUSE 34 136
DBREF 4WIL B 1 103 UNP Q9CZL5 PHS2_MOUSE 34 136
SEQADV 4WIL GLY A -1 UNP Q9CZL5 EXPRESSION TAG
SEQADV 4WIL SER A 0 UNP Q9CZL5 EXPRESSION TAG
SEQADV 4WIL THR A 51 UNP Q9CZL5 SER 84 ENGINEERED MUTATION
SEQADV 4WIL GLY B -1 UNP Q9CZL5 EXPRESSION TAG
SEQADV 4WIL SER B 0 UNP Q9CZL5 EXPRESSION TAG
SEQADV 4WIL THR B 51 UNP Q9CZL5 SER 84 ENGINEERED MUTATION
SEQRES 1 A 105 GLY SER MET SER SER ASP ALA GLN TRP LEU THR ALA GLU
SEQRES 2 A 105 GLU ARG ASP GLN LEU ILE PRO GLY LEU LYS ALA ALA GLY
SEQRES 3 A 105 TRP SER GLU LEU SER GLU ARG ASP ALA ILE TYR LYS GLU
SEQRES 4 A 105 PHE SER PHE LYS ASN PHE ASN GLN ALA PHE GLY PHE MET
SEQRES 5 A 105 THR ARG VAL ALA LEU GLN ALA GLU LYS MET ASN HIS HIS
SEQRES 6 A 105 PRO GLU TRP PHE ASN VAL TYR ASN LYS VAL GLN ILE THR
SEQRES 7 A 105 LEU THR SER HIS ASP CYS GLY GLY LEU THR LYS ARG ASP
SEQRES 8 A 105 VAL LYS LEU ALA GLN PHE ILE GLU LYS ALA ALA ALA SER
SEQRES 9 A 105 LEU
SEQRES 1 B 105 GLY SER MET SER SER ASP ALA GLN TRP LEU THR ALA GLU
SEQRES 2 B 105 GLU ARG ASP GLN LEU ILE PRO GLY LEU LYS ALA ALA GLY
SEQRES 3 B 105 TRP SER GLU LEU SER GLU ARG ASP ALA ILE TYR LYS GLU
SEQRES 4 B 105 PHE SER PHE LYS ASN PHE ASN GLN ALA PHE GLY PHE MET
SEQRES 5 B 105 THR ARG VAL ALA LEU GLN ALA GLU LYS MET ASN HIS HIS
SEQRES 6 B 105 PRO GLU TRP PHE ASN VAL TYR ASN LYS VAL GLN ILE THR
SEQRES 7 B 105 LEU THR SER HIS ASP CYS GLY GLY LEU THR LYS ARG ASP
SEQRES 8 B 105 VAL LYS LEU ALA GLN PHE ILE GLU LYS ALA ALA ALA SER
SEQRES 9 B 105 LEU
FORMUL 3 HOH *214(H2 O)
HELIX 1 AA1 THR A 9 ALA A 23 1 15
HELIX 2 AA2 ASN A 42 ASN A 61 1 20
HELIX 3 AA3 THR A 86 ALA A 101 1 16
HELIX 4 AA4 THR B 9 ALA B 23 1 15
HELIX 5 AA5 ASN B 42 ASN B 61 1 20
HELIX 6 AA6 THR B 86 ALA B 101 1 16
SHEET 1 AA1 8 SER A 26 GLU A 27 0
SHEET 2 AA1 8 ILE A 34 SER A 39 -1 O TYR A 35 N SER A 26
SHEET 3 AA1 8 LYS A 72 LEU A 77 -1 O VAL A 73 N PHE A 38
SHEET 4 AA1 8 GLU A 65 VAL A 69 -1 N PHE A 67 O GLN A 74
SHEET 5 AA1 8 GLU B 65 VAL B 69 -1 O ASN B 68 N TRP A 66
SHEET 6 AA1 8 LYS B 72 LEU B 77 -1 O THR B 76 N GLU B 65
SHEET 7 AA1 8 ILE B 34 SER B 39 -1 N PHE B 38 O VAL B 73
SHEET 8 AA1 8 SER B 26 GLU B 27 -1 N SER B 26 O TYR B 35
CRYST1 57.729 57.729 115.064 90.00 90.00 120.00 P 31 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 0.017322 0.010001 0.000000 0.00000
SCALE2 0.000000 0.020002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008691 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
