HEADER PROTEIN BINDING 17-OCT-14 4WPE
TITLE CRYSTAL STRUCTURE OF HOF1P F-BAR DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOKINESIS PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HOMOLOG OF CDC15 PROTEIN 1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: HOF1, CYK2, YMR032W, YM9973.05;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: B834
KEYWDS F-BAR DOMAIN, MEMBRANE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.LEMMON,K.MORAVCEVIC
REVDAT 4 27-DEC-23 4WPE 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 18-FEB-15 4WPE 1 JRNL
REVDAT 2 11-FEB-15 4WPE 1 JRNL
REVDAT 1 24-DEC-14 4WPE 0
JRNL AUTH K.MORAVCEVIC,D.ALVARADO,K.R.SCHMITZ,J.A.KENNISTON,
JRNL AUTH 2 J.M.MENDROLA,K.M.FERGUSON,M.A.LEMMON
JRNL TITL COMPARISON OF SACCHAROMYCES CEREVISIAE F-BAR DOMAIN
JRNL TITL 2 STRUCTURES REVEALS A CONSERVED INOSITOL PHOSPHATE BINDING
JRNL TITL 3 SITE.
JRNL REF STRUCTURE V. 23 352 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25620000
JRNL DOI 10.1016/J.STR.2014.12.009
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 11429
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 546
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 39.9119 - 4.2838 1.00 2839 134 0.1919 0.2035
REMARK 3 2 4.2838 - 3.4008 1.00 2752 143 0.1944 0.2311
REMARK 3 3 3.4008 - 2.9710 0.99 2747 132 0.2549 0.3481
REMARK 3 4 2.9710 - 2.6995 0.94 2545 137 0.2496 0.3142
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 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 : 0.003 2221
REMARK 3 ANGLE : 0.607 2988
REMARK 3 CHIRALITY : 0.023 328
REMARK 3 PLANARITY : 0.002 387
REMARK 3 DIHEDRAL : 15.425 815
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3817 39.7422 61.4186
REMARK 3 T TENSOR
REMARK 3 T11: 0.3968 T22: 0.6041
REMARK 3 T33: 0.4414 T12: -0.1109
REMARK 3 T13: -0.0018 T23: -0.1177
REMARK 3 L TENSOR
REMARK 3 L11: -0.0161 L22: 0.0341
REMARK 3 L33: 0.2811 L12: -0.1199
REMARK 3 L13: -0.2250 L23: -0.1780
REMARK 3 S TENSOR
REMARK 3 S11: -0.1144 S12: 0.1975 S13: -0.0118
REMARK 3 S21: -0.0059 S22: -0.1456 S23: 0.0413
REMARK 3 S31: 0.0771 S32: -0.0257 S33: -0.0196
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 4WPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11489
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.9000
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: MAD
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 (%): 58.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA CITRATE, PH 5.5, CONTAINING
REMARK 280 0.1 M AMMONIUM ACETATE, AND 5-7% (W/V) PEG3350, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 68.58900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.94650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.58900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.94650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 7960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 -1.000000 0.000000 0.000000 71.15731
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 69.49838
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 417 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 MSE A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 276
REMARK 465 LYS A 277
REMARK 465 THR A 278
REMARK 465 SER A 279
REMARK 465 LYS A 280
REMARK 465 GLY A 281
REMARK 465 ASP A 282
REMARK 465 MSE A 283
REMARK 465 ASN A 284
REMARK 465 SER A 285
REMARK 465 SER A 286
REMARK 465 ALA A 287
REMARK 465 ASN A 288
REMARK 465 TRP A 289
REMARK 465 ALA A 290
REMARK 465 GLN A 291
REMARK 465 MSE A 292
REMARK 465 SER A 293
REMARK 465 SER A 294
REMARK 465 ILE A 295
REMARK 465 SER A 296
REMARK 465 THR A 297
REMARK 465 THR A 298
REMARK 465 SER A 299
REMARK 465 LYS A 300
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 11 CG OD1 OD2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 LEU A 72 CG CD1 CD2
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 GLU A 124 CG CD OE1 OE2
REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 GLN A 145 CG CD OE1 NE2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 ARG A 166 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 171 CG CD CE NZ
REMARK 470 LYS A 200 CG CD CE NZ
REMARK 470 LYS A 275 CG CD CE NZ
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 2 116.78 4.53
REMARK 500 ILE A 162 -64.48 -98.09
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4WPE A 2 300 UNP Q05080 CYK2_YEAST 2 300
SEQADV 4WPE MSE A -5 UNP Q05080 INITIATING METHIONINE
SEQADV 4WPE HIS A -4 UNP Q05080 EXPRESSION TAG
SEQADV 4WPE HIS A -3 UNP Q05080 EXPRESSION TAG
SEQADV 4WPE HIS A -2 UNP Q05080 EXPRESSION TAG
SEQADV 4WPE HIS A -1 UNP Q05080 EXPRESSION TAG
SEQADV 4WPE HIS A 0 UNP Q05080 EXPRESSION TAG
SEQADV 4WPE HIS A 1 UNP Q05080 EXPRESSION TAG
SEQRES 1 A 306 MSE HIS HIS HIS HIS HIS HIS SER TYR SER TYR GLU ALA
SEQRES 2 A 306 CYS PHE TRP ASP PRO ASN ASP ASN GLY VAL ASN ILE LEU
SEQRES 3 A 306 LEU GLY HIS ILE SER GLN GLY ILE ARG SER CYS ASP SER
SEQRES 4 A 306 MSE ILE LEU PHE PHE LYS GLN ARG SER GLU LEU GLU LYS
SEQRES 5 A 306 ASP TYR ALA ARG ARG LEU GLY ALA ILE THR GLY LYS LEU
SEQRES 6 A 306 ASP LYS ASP ILE GLY THR ASN MSE ASP TYR GLY LYS LEU
SEQRES 7 A 306 ASN GLU THR PHE ASN VAL VAL LEU SER VAL GLU LYS ALA
SEQRES 8 A 306 ARG ALA GLN SER HIS SER LYS GLN SER GLU ILE LEU PHE
SEQRES 9 A 306 ARG GLN ILE TYR THR ASP THR LYS ALA PHE ALA ALA ASN
SEQRES 10 A 306 LEU GLN ALA ARG TYR THR THR LEU SER GLY LYS ILE GLU
SEQRES 11 A 306 ARG LEU ARG MSE ASP LYS PHE ASN LYS LYS LYS GLY CYS
SEQRES 12 A 306 GLU VAL LEU GLN LYS LYS LEU GLN ASP ALA GLN ILE ARG
SEQRES 13 A 306 PHE ARG ASP LEU GLN LEU ASN GLU ASN ASN MSE ILE GLY
SEQRES 14 A 306 ALA LYS ARG VAL GLU HIS ASN LYS ARG GLU LEU LEU LYS
SEQRES 15 A 306 TRP GLU SER ASN SER GLN GLU TYR LYS VAL GLN LEU ASP
SEQRES 16 A 306 VAL LEU LYS GLN GLU TYR LYS ALA SER GLN LYS PHE TRP
SEQRES 17 A 306 ILE HIS GLU TRP ALA GLN LEU SER CYS GLU LEU GLN GLU
SEQRES 18 A 306 MSE GLU ASN ALA ARG ILE SER PHE LEU GLN SER LYS LEU
SEQRES 19 A 306 GLN GLN PHE ALA THR SER SER MSE GLU THR TYR ILE LEU
SEQRES 20 A 306 GLU GLN THR LYS MSE ASP MSE LEU THR ASN HIS LEU ASN
SEQRES 21 A 306 SER PHE THR ALA ALA ASP GLU ILE SER THR PHE SER LYS
SEQRES 22 A 306 GLU ASN GLY THR GLY ARG LEU LYS HIS LYS THR SER LYS
SEQRES 23 A 306 GLY ASP MSE ASN SER SER ALA ASN TRP ALA GLN MSE SER
SEQRES 24 A 306 SER ILE SER THR THR SER LYS
MODRES 4WPE MSE A 34 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 67 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 128 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 161 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 216 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 236 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 246 MET MODIFIED RESIDUE
MODRES 4WPE MSE A 248 MET MODIFIED RESIDUE
HET MSE A 34 8
HET MSE A 67 8
HET MSE A 128 8
HET MSE A 161 8
HET MSE A 216 8
HET MSE A 236 8
HET MSE A 246 8
HET MSE A 248 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 HOH *40(H2 O)
HELIX 1 AA1 SER A 4 PHE A 9 1 6
HELIX 2 AA2 ASP A 14 SER A 30 1 17
HELIX 3 AA3 SER A 30 ASN A 66 1 37
HELIX 4 AA4 TYR A 69 GLN A 100 1 32
HELIX 5 AA5 ILE A 101 ASN A 157 1 57
HELIX 6 AA6 GLU A 158 MSE A 161 5 4
HELIX 7 AA7 GLY A 163 ASN A 254 1 92
HELIX 8 AA8 THR A 257 GLY A 270 1 14
LINK C SER A 33 N MSE A 34 1555 1555 1.33
LINK C MSE A 34 N ILE A 35 1555 1555 1.33
LINK C ASN A 66 N MSE A 67 1555 1555 1.33
LINK C MSE A 67 N ASP A 68 1555 1555 1.33
LINK C ARG A 127 N MSE A 128 1555 1555 1.33
LINK C MSE A 128 N ASP A 129 1555 1555 1.33
LINK C ASN A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N ILE A 162 1555 1555 1.33
LINK C GLU A 215 N MSE A 216 1555 1555 1.33
LINK C MSE A 216 N GLU A 217 1555 1555 1.33
LINK C SER A 235 N MSE A 236 1555 1555 1.33
LINK C MSE A 236 N GLU A 237 1555 1555 1.33
LINK C LYS A 245 N MSE A 246 1555 1555 1.33
LINK C MSE A 246 N ASP A 247 1555 1555 1.33
LINK C ASP A 247 N MSE A 248 1555 1555 1.33
LINK C MSE A 248 N LEU A 249 1555 1555 1.33
CRYST1 137.178 43.893 95.858 90.00 133.53 90.00 C 1 2 1 4
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 0.007290 0.000000 0.006925 0.00000
SCALE2 0.000000 0.022783 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014388 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
