HEADER STRUCTURAL PROTEIN 23-JAN-07 2OND
TITLE CRYSTAL STRUCTURE OF THE HAT-C DOMAIN OF MURINE CSTF-77
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLEAVAGE STIMULATION FACTOR 77 KDA SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 242-549;
COMPND 5 SYNONYM: CSTF 77 KDA SUBUNIT, CF-1 77 KDA SUBUNIT, CSTF-77;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CSTF3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28A;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PLASMID
KEYWDS HAT DOMAIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BAI,T.C.AUPERIN,C.-Y.CHOU,G.-G.CHANG,J.L.MANLEY,L.TONG
REVDAT 4 27-DEC-23 2OND 1 SEQADV LINK
REVDAT 3 18-OCT-17 2OND 1 REMARK
REVDAT 2 24-FEB-09 2OND 1 VERSN
REVDAT 1 10-APR-07 2OND 0
JRNL AUTH Y.BAI,T.C.AUPERIN,C.Y.CHOU,G.G.CHANG,J.L.MANLEY,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF MURINE CSTF-77: DIMERIC ASSOCIATION AND
JRNL TITL 2 IMPLICATIONS FOR POLYADENYLATION OF MRNA PRECURSORS.
JRNL REF MOL.CELL V. 25 863 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17386263
JRNL DOI 10.1016/J.MOLCEL.2007.01.034
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 360403.580
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 52247
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) : 0.224
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.400
REMARK 3 FREE R VALUE TEST SET COUNT : 3852
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4608
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE : 0.4130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 338
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5099
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : -1.29000
REMARK 3 B12 (A**2) : 8.86000
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) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.42
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.750
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) : 1.380 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.370 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.400 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.490 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 35.31
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 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.5688
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB THEN SOLVE/RESOLVE, SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WITH PROTEASE (SUBTILISIN) IN THE
REMARK 280 DROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 53.86667
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 107.73333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 80.80000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 134.66667
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 26.93333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.86667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 107.73333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 134.66667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 80.80000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 26.93333
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: 5370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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 SER A 261 34.35 -83.14
REMARK 500 ASN A 262 69.09 30.23
REMARK 500 THR A 266 -174.81 -65.38
REMARK 500 LYS A 311 35.93 -92.65
REMARK 500 THR A 334 -89.83 -150.19
REMARK 500 GLU A 515 -75.95 -49.96
REMARK 500 LYS A 519 44.66 -142.41
REMARK 500 MSE A 531 90.04 15.38
REMARK 500 LEU B 264 61.54 -109.89
REMARK 500 ARG B 265 110.14 -8.02
REMARK 500 THR B 270 -16.94 -48.41
REMARK 500 ASP B 313 83.83 -59.19
REMARK 500 THR B 334 -85.97 -121.19
REMARK 500 GLU B 514 -77.78 -54.11
REMARK 500 GLU B 515 -86.45 -23.46
REMARK 500 MSE B 531 69.51 25.36
REMARK 500 ASP B 532 -3.91 89.24
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2OND A 242 549 UNP Q99LI7 CSTF3_MOUSE 242 549
DBREF 2OND B 242 549 UNP Q99LI7 CSTF3_MOUSE 242 549
SEQADV 2OND MSE A 251 UNP Q99LI7 MET 251 MODIFIED RESIDUE
SEQADV 2OND MSE A 277 UNP Q99LI7 MET 277 MODIFIED RESIDUE
SEQADV 2OND MSE A 314 UNP Q99LI7 MET 314 MODIFIED RESIDUE
SEQADV 2OND MSE A 340 UNP Q99LI7 MET 340 MODIFIED RESIDUE
SEQADV 2OND MSE A 354 UNP Q99LI7 MET 354 MODIFIED RESIDUE
SEQADV 2OND MSE A 382 UNP Q99LI7 MET 382 MODIFIED RESIDUE
SEQADV 2OND MSE A 396 UNP Q99LI7 MET 396 MODIFIED RESIDUE
SEQADV 2OND MSE A 418 UNP Q99LI7 MET 418 MODIFIED RESIDUE
SEQADV 2OND MSE A 531 UNP Q99LI7 MET 531 MODIFIED RESIDUE
SEQADV 2OND MSE B 251 UNP Q99LI7 MET 251 MODIFIED RESIDUE
SEQADV 2OND MSE B 277 UNP Q99LI7 MET 277 MODIFIED RESIDUE
SEQADV 2OND MSE B 314 UNP Q99LI7 MET 314 MODIFIED RESIDUE
SEQADV 2OND MSE B 340 UNP Q99LI7 MET 340 MODIFIED RESIDUE
SEQADV 2OND MSE B 354 UNP Q99LI7 MET 354 MODIFIED RESIDUE
SEQADV 2OND MSE B 382 UNP Q99LI7 MET 382 MODIFIED RESIDUE
SEQADV 2OND MSE B 396 UNP Q99LI7 MET 396 MODIFIED RESIDUE
SEQADV 2OND MSE B 418 UNP Q99LI7 MET 418 MODIFIED RESIDUE
SEQADV 2OND MSE B 531 UNP Q99LI7 MET 531 MODIFIED RESIDUE
SEQRES 1 A 308 THR PRO GLN GLU ALA GLN GLN VAL ASP MSE TRP LYS LYS
SEQRES 2 A 308 TYR ILE GLN TRP GLU LYS SER ASN PRO LEU ARG THR GLU
SEQRES 3 A 308 ASP GLN THR LEU ILE THR LYS ARG VAL MSE PHE ALA TYR
SEQRES 4 A 308 GLU GLN CYS LEU LEU VAL LEU GLY HIS HIS PRO ASP ILE
SEQRES 5 A 308 TRP TYR GLU ALA ALA GLN TYR LEU GLU GLN SER SER LYS
SEQRES 6 A 308 LEU LEU ALA GLU LYS GLY ASP MSE ASN ASN ALA LYS LEU
SEQRES 7 A 308 PHE SER ASP GLU ALA ALA ASN ILE TYR GLU ARG ALA ILE
SEQRES 8 A 308 SER THR LEU LEU LYS LYS ASN MSE LEU LEU TYR PHE ALA
SEQRES 9 A 308 TYR ALA ASP TYR GLU GLU SER ARG MSE LYS TYR GLU LYS
SEQRES 10 A 308 VAL HIS SER ILE TYR ASN ARG LEU LEU ALA ILE GLU ASP
SEQRES 11 A 308 ILE ASP PRO THR LEU VAL TYR ILE GLN TYR MSE LYS PHE
SEQRES 12 A 308 ALA ARG ARG ALA GLU GLY ILE LYS SER GLY ARG MSE ILE
SEQRES 13 A 308 PHE LYS LYS ALA ARG GLU ASP ALA ARG THR ARG HIS HIS
SEQRES 14 A 308 VAL TYR VAL THR ALA ALA LEU MSE GLU TYR TYR CYS SER
SEQRES 15 A 308 LYS ASP LYS SER VAL ALA PHE LYS ILE PHE GLU LEU GLY
SEQRES 16 A 308 LEU LYS LYS TYR GLY ASP ILE PRO GLU TYR VAL LEU ALA
SEQRES 17 A 308 TYR ILE ASP TYR LEU SER HIS LEU ASN GLU ASP ASN ASN
SEQRES 18 A 308 THR ARG VAL LEU PHE GLU ARG VAL LEU THR SER GLY SER
SEQRES 19 A 308 LEU PRO PRO GLU LYS SER GLY GLU ILE TRP ALA ARG PHE
SEQRES 20 A 308 LEU ALA PHE GLU SER ASN ILE GLY ASP LEU ALA SER ILE
SEQRES 21 A 308 LEU LYS VAL GLU LYS ARG ARG PHE THR ALA PHE ARG GLU
SEQRES 22 A 308 GLU TYR GLU GLY LYS GLU THR ALA LEU LEU VAL ASP ARG
SEQRES 23 A 308 TYR LYS PHE MSE ASP LEU TYR PRO CYS SER ALA SER GLU
SEQRES 24 A 308 LEU LYS ALA LEU GLY TYR LYS ASP VAL
SEQRES 1 B 308 THR PRO GLN GLU ALA GLN GLN VAL ASP MSE TRP LYS LYS
SEQRES 2 B 308 TYR ILE GLN TRP GLU LYS SER ASN PRO LEU ARG THR GLU
SEQRES 3 B 308 ASP GLN THR LEU ILE THR LYS ARG VAL MSE PHE ALA TYR
SEQRES 4 B 308 GLU GLN CYS LEU LEU VAL LEU GLY HIS HIS PRO ASP ILE
SEQRES 5 B 308 TRP TYR GLU ALA ALA GLN TYR LEU GLU GLN SER SER LYS
SEQRES 6 B 308 LEU LEU ALA GLU LYS GLY ASP MSE ASN ASN ALA LYS LEU
SEQRES 7 B 308 PHE SER ASP GLU ALA ALA ASN ILE TYR GLU ARG ALA ILE
SEQRES 8 B 308 SER THR LEU LEU LYS LYS ASN MSE LEU LEU TYR PHE ALA
SEQRES 9 B 308 TYR ALA ASP TYR GLU GLU SER ARG MSE LYS TYR GLU LYS
SEQRES 10 B 308 VAL HIS SER ILE TYR ASN ARG LEU LEU ALA ILE GLU ASP
SEQRES 11 B 308 ILE ASP PRO THR LEU VAL TYR ILE GLN TYR MSE LYS PHE
SEQRES 12 B 308 ALA ARG ARG ALA GLU GLY ILE LYS SER GLY ARG MSE ILE
SEQRES 13 B 308 PHE LYS LYS ALA ARG GLU ASP ALA ARG THR ARG HIS HIS
SEQRES 14 B 308 VAL TYR VAL THR ALA ALA LEU MSE GLU TYR TYR CYS SER
SEQRES 15 B 308 LYS ASP LYS SER VAL ALA PHE LYS ILE PHE GLU LEU GLY
SEQRES 16 B 308 LEU LYS LYS TYR GLY ASP ILE PRO GLU TYR VAL LEU ALA
SEQRES 17 B 308 TYR ILE ASP TYR LEU SER HIS LEU ASN GLU ASP ASN ASN
SEQRES 18 B 308 THR ARG VAL LEU PHE GLU ARG VAL LEU THR SER GLY SER
SEQRES 19 B 308 LEU PRO PRO GLU LYS SER GLY GLU ILE TRP ALA ARG PHE
SEQRES 20 B 308 LEU ALA PHE GLU SER ASN ILE GLY ASP LEU ALA SER ILE
SEQRES 21 B 308 LEU LYS VAL GLU LYS ARG ARG PHE THR ALA PHE ARG GLU
SEQRES 22 B 308 GLU TYR GLU GLY LYS GLU THR ALA LEU LEU VAL ASP ARG
SEQRES 23 B 308 TYR LYS PHE MSE ASP LEU TYR PRO CYS SER ALA SER GLU
SEQRES 24 B 308 LEU LYS ALA LEU GLY TYR LYS ASP VAL
MODRES 2OND MSE A 251 MET SELENOMETHIONINE
MODRES 2OND MSE A 277 MET SELENOMETHIONINE
MODRES 2OND MSE A 314 MET SELENOMETHIONINE
MODRES 2OND MSE A 340 MET SELENOMETHIONINE
MODRES 2OND MSE A 354 MET SELENOMETHIONINE
MODRES 2OND MSE A 382 MET SELENOMETHIONINE
MODRES 2OND MSE A 396 MET SELENOMETHIONINE
MODRES 2OND MSE A 418 MET SELENOMETHIONINE
MODRES 2OND MSE A 531 MET SELENOMETHIONINE
MODRES 2OND MSE B 251 MET SELENOMETHIONINE
MODRES 2OND MSE B 277 MET SELENOMETHIONINE
MODRES 2OND MSE B 314 MET SELENOMETHIONINE
MODRES 2OND MSE B 340 MET SELENOMETHIONINE
MODRES 2OND MSE B 354 MET SELENOMETHIONINE
MODRES 2OND MSE B 382 MET SELENOMETHIONINE
MODRES 2OND MSE B 396 MET SELENOMETHIONINE
MODRES 2OND MSE B 418 MET SELENOMETHIONINE
MODRES 2OND MSE B 531 MET SELENOMETHIONINE
HET MSE A 251 8
HET MSE A 277 8
HET MSE A 314 8
HET MSE A 340 8
HET MSE A 354 8
HET MSE A 382 8
HET MSE A 396 8
HET MSE A 418 8
HET MSE A 531 8
HET MSE B 251 8
HET MSE B 277 8
HET MSE B 314 8
HET MSE B 340 8
HET MSE B 354 8
HET MSE B 382 8
HET MSE B 396 8
HET MSE B 418 8
HET MSE B 531 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 18(C5 H11 N O2 SE)
HELIX 1 1 THR A 242 SER A 261 1 20
HELIX 2 2 ASP A 268 GLY A 288 1 21
HELIX 3 3 HIS A 290 LYS A 311 1 22
HELIX 4 4 MSE A 314 SER A 333 1 20
HELIX 5 5 ASN A 339 ARG A 353 1 15
HELIX 6 6 LYS A 355 ALA A 368 1 14
HELIX 7 7 PRO A 374 GLY A 390 1 17
HELIX 8 8 GLY A 390 GLU A 403 1 14
HELIX 9 9 HIS A 409 CYS A 422 1 14
HELIX 10 10 ASP A 425 GLY A 441 1 17
HELIX 11 11 ILE A 443 HIS A 456 1 14
HELIX 12 12 GLU A 459 SER A 473 1 15
HELIX 13 13 PRO A 477 LYS A 480 5 4
HELIX 14 14 SER A 481 GLY A 496 1 16
HELIX 15 15 ASP A 497 PHE A 512 1 16
HELIX 16 16 LYS A 519 ASP A 526 1 8
HELIX 17 17 SER A 537 ALA A 543 1 7
HELIX 18 18 THR B 242 SER B 261 1 20
HELIX 19 19 ASP B 268 GLY B 288 1 21
HELIX 20 20 HIS B 290 GLU B 310 1 21
HELIX 21 21 ASP B 313 THR B 334 1 22
HELIX 22 22 ASN B 339 ARG B 353 1 15
HELIX 23 23 LYS B 355 ALA B 368 1 14
HELIX 24 24 PRO B 374 GLY B 390 1 17
HELIX 25 25 GLY B 390 ASP B 404 1 15
HELIX 26 26 HIS B 409 CYS B 422 1 14
HELIX 27 27 ASP B 425 GLY B 441 1 17
HELIX 28 28 ILE B 443 HIS B 456 1 14
HELIX 29 29 GLU B 459 SER B 473 1 15
HELIX 30 30 PRO B 477 LYS B 480 5 4
HELIX 31 31 SER B 481 GLY B 496 1 16
HELIX 32 32 ASP B 497 ALA B 511 1 15
HELIX 33 33 LYS B 519 LYS B 529 1 11
HELIX 34 34 SER B 537 LEU B 544 1 8
LINK C ASP A 250 N MSE A 251 1555 1555 1.33
LINK C MSE A 251 N TRP A 252 1555 1555 1.32
LINK C VAL A 276 N MSE A 277 1555 1555 1.33
LINK C MSE A 277 N PHE A 278 1555 1555 1.33
LINK C ASP A 313 N MSE A 314 1555 1555 1.33
LINK C MSE A 314 N ASN A 315 1555 1555 1.33
LINK C ASN A 339 N MSE A 340 1555 1555 1.33
LINK C MSE A 340 N LEU A 341 1555 1555 1.33
LINK C ARG A 353 N MSE A 354 1555 1555 1.33
LINK C MSE A 354 N LYS A 355 1555 1555 1.33
LINK C TYR A 381 N MSE A 382 1555 1555 1.33
LINK C MSE A 382 N LYS A 383 1555 1555 1.33
LINK C ARG A 395 N MSE A 396 1555 1555 1.33
LINK C MSE A 396 N ILE A 397 1555 1555 1.33
LINK C LEU A 417 N MSE A 418 1555 1555 1.33
LINK C MSE A 418 N GLU A 419 1555 1555 1.33
LINK C PHE A 530 N MSE A 531 1555 1555 1.33
LINK C MSE A 531 N ASP A 532 1555 1555 1.32
LINK C ASP B 250 N MSE B 251 1555 1555 1.33
LINK C MSE B 251 N TRP B 252 1555 1555 1.33
LINK C VAL B 276 N MSE B 277 1555 1555 1.33
LINK C MSE B 277 N PHE B 278 1555 1555 1.33
LINK C ASP B 313 N MSE B 314 1555 1555 1.33
LINK C MSE B 314 N ASN B 315 1555 1555 1.33
LINK C ASN B 339 N MSE B 340 1555 1555 1.33
LINK C MSE B 340 N LEU B 341 1555 1555 1.33
LINK C ARG B 353 N MSE B 354 1555 1555 1.33
LINK C MSE B 354 N LYS B 355 1555 1555 1.32
LINK C TYR B 381 N MSE B 382 1555 1555 1.33
LINK C MSE B 382 N LYS B 383 1555 1555 1.33
LINK C ARG B 395 N MSE B 396 1555 1555 1.33
LINK C MSE B 396 N ILE B 397 1555 1555 1.33
LINK C LEU B 417 N MSE B 418 1555 1555 1.33
LINK C MSE B 418 N GLU B 419 1555 1555 1.33
LINK C PHE B 530 N MSE B 531 1555 1555 1.33
LINK C MSE B 531 N ASP B 532 1555 1555 1.33
CRYST1 155.400 155.400 161.600 90.00 90.00 120.00 P 61 2 2 24
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 0.006435 0.003715 0.000000 0.00000
SCALE2 0.000000 0.007431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006188 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
