HEADER CHAPERONE 27-AUG-04 1WP0
TITLE HUMAN SCO1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCO1 PROTEIN HOMOLOG;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: IMS FRAGMENT;
COMPND 5 SYNONYM: HSCO1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET24D
KEYWDS CU-BINDING PROTEIN, MITOCHONDRIAL ASSEMBLY FACTOR, REDOX,
KEYWDS 2 CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.C.WILLIAMS,C.SUE,G.S.BANTING,H.YANG,D.M.GLERUM,
AUTHOR 2 W.A.HENDRICKSON,E.A.SCHON
REVDAT 3 24-FEB-09 1WP0 1 VERSN
REVDAT 2 19-APR-05 1WP0 1 JRNL
REVDAT 1 18-JAN-05 1WP0 0
JRNL AUTH J.C.WILLIAMS,C.SUE,G.S.BANTING,H.YANG,D.M.GLERUM,
JRNL AUTH 2 W.A.HENDRICKSON,E.A.SCHON
JRNL TITL CRYSTAL STRUCTURE OF HUMAN SCO1: IMPLICATIONS FOR
JRNL TITL 2 REDOX SIGNALING BY A MITOCHONDRIAL CYTOCHROME C
JRNL TITL 3 OXIDASE "ASSEMBLY" PROTEIN
JRNL REF J.BIOL.CHEM. V. 280 15202 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15659396
JRNL DOI 10.1074/JBC.M410705200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 28470
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1463
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3883
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 26
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WP0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB023833.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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) : 0.97887, 0.97928, 0.96864,
REMARK 200 0.98713
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 30575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
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: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, 200MM NASCN, 5% XYLITOL,
REMARK 280 PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 30.10500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.58400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.57700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.58400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.10500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.57700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 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 137
REMARK 465 ARG A 298
REMARK 465 LYS A 299
REMARK 465 LYS A 300
REMARK 465 SER A 301
REMARK 465 ARG B 298
REMARK 465 LYS B 299
REMARK 465 LYS B 300
REMARK 465 SER B 301
REMARK 465 ARG C 298
REMARK 465 LYS C 299
REMARK 465 LYS C 300
REMARK 465 SER C 301
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 PRO A 194 -173.29 -59.99
REMARK 500 SER A 221 139.62 171.37
REMARK 500 ASP A 251 -161.13 -72.56
REMARK 500 HIS B 145 1.94 -67.45
REMARK 500 ASP B 171 -67.41 -108.42
REMARK 500 PRO B 194 -175.15 -63.91
REMARK 500 ASP B 208 89.39 -61.62
REMARK 500 SER B 221 152.02 179.12
REMARK 500 GLU B 252 64.72 -68.83
REMARK 500 ASP B 253 8.58 -178.30
REMARK 500 TYR B 256 148.19 -178.29
REMARK 500 PRO B 296 5.41 -63.97
REMARK 500 ASP C 171 -50.24 -126.37
REMARK 500 PRO C 194 -168.51 -57.16
REMARK 500 SER C 221 150.02 179.13
REMARK 500 ASP C 253 14.37 86.57
REMARK 500 GLU C 254 7.67 51.34
REMARK 500 LEU C 274 -33.65 -141.54
REMARK 500 PRO C 296 -82.60 -54.01
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WP0 A 138 301 UNP O75880 SCO1_HUMAN 138 301
DBREF 1WP0 B 138 301 UNP O75880 SCO1_HUMAN 138 301
DBREF 1WP0 C 138 301 UNP O75880 SCO1_HUMAN 138 301
SEQADV 1WP0 MSE A 137 UNP O75880 INITIATING METHIONINE
SEQADV 1WP0 MSE A 180 UNP O75880 MET 180 MODIFIED RESIDUE
SEQADV 1WP0 MSE A 264 UNP O75880 MET 264 MODIFIED RESIDUE
SEQADV 1WP0 MSE A 294 UNP O75880 MET 294 MODIFIED RESIDUE
SEQADV 1WP0 MSE B 137 UNP O75880 INITIATING METHIONINE
SEQADV 1WP0 MSE B 180 UNP O75880 MET 180 MODIFIED RESIDUE
SEQADV 1WP0 MSE B 264 UNP O75880 MET 264 MODIFIED RESIDUE
SEQADV 1WP0 MSE B 294 UNP O75880 MET 294 MODIFIED RESIDUE
SEQADV 1WP0 MSE C 137 UNP O75880 INITIATING METHIONINE
SEQADV 1WP0 MSE C 180 UNP O75880 MET 180 MODIFIED RESIDUE
SEQADV 1WP0 MSE C 264 UNP O75880 MET 264 MODIFIED RESIDUE
SEQADV 1WP0 MSE C 294 UNP O75880 MET 294 MODIFIED RESIDUE
SEQRES 1 A 165 MSE GLY PRO PHE SER LEU THR THR HIS THR GLY GLU ARG
SEQRES 2 A 165 LYS THR ASP LYS ASP TYR LEU GLY GLN TRP LEU LEU ILE
SEQRES 3 A 165 TYR PHE GLY PHE THR HIS CYS PRO ASP VAL CYS PRO GLU
SEQRES 4 A 165 GLU LEU GLU LYS MSE ILE GLN VAL VAL ASP GLU ILE ASP
SEQRES 5 A 165 SER ILE THR THR LEU PRO ASP LEU THR PRO LEU PHE ILE
SEQRES 6 A 165 SER ILE ASP PRO GLU ARG ASP THR LYS GLU ALA ILE ALA
SEQRES 7 A 165 ASN TYR VAL LYS GLU PHE SER PRO LYS LEU VAL GLY LEU
SEQRES 8 A 165 THR GLY THR ARG GLU GLU VAL ASP GLN VAL ALA ARG ALA
SEQRES 9 A 165 TYR ARG VAL TYR TYR SER PRO GLY PRO LYS ASP GLU ASP
SEQRES 10 A 165 GLU ASP TYR ILE VAL ASP HIS THR ILE ILE MSE TYR LEU
SEQRES 11 A 165 ILE GLY PRO ASP GLY GLU PHE LEU ASP TYR PHE GLY GLN
SEQRES 12 A 165 ASN LYS ARG LYS GLY GLU ILE ALA ALA SER ILE ALA THR
SEQRES 13 A 165 HIS MSE ARG PRO TYR ARG LYS LYS SER
SEQRES 1 B 165 MSE GLY PRO PHE SER LEU THR THR HIS THR GLY GLU ARG
SEQRES 2 B 165 LYS THR ASP LYS ASP TYR LEU GLY GLN TRP LEU LEU ILE
SEQRES 3 B 165 TYR PHE GLY PHE THR HIS CYS PRO ASP VAL CYS PRO GLU
SEQRES 4 B 165 GLU LEU GLU LYS MSE ILE GLN VAL VAL ASP GLU ILE ASP
SEQRES 5 B 165 SER ILE THR THR LEU PRO ASP LEU THR PRO LEU PHE ILE
SEQRES 6 B 165 SER ILE ASP PRO GLU ARG ASP THR LYS GLU ALA ILE ALA
SEQRES 7 B 165 ASN TYR VAL LYS GLU PHE SER PRO LYS LEU VAL GLY LEU
SEQRES 8 B 165 THR GLY THR ARG GLU GLU VAL ASP GLN VAL ALA ARG ALA
SEQRES 9 B 165 TYR ARG VAL TYR TYR SER PRO GLY PRO LYS ASP GLU ASP
SEQRES 10 B 165 GLU ASP TYR ILE VAL ASP HIS THR ILE ILE MSE TYR LEU
SEQRES 11 B 165 ILE GLY PRO ASP GLY GLU PHE LEU ASP TYR PHE GLY GLN
SEQRES 12 B 165 ASN LYS ARG LYS GLY GLU ILE ALA ALA SER ILE ALA THR
SEQRES 13 B 165 HIS MSE ARG PRO TYR ARG LYS LYS SER
SEQRES 1 C 165 MSE GLY PRO PHE SER LEU THR THR HIS THR GLY GLU ARG
SEQRES 2 C 165 LYS THR ASP LYS ASP TYR LEU GLY GLN TRP LEU LEU ILE
SEQRES 3 C 165 TYR PHE GLY PHE THR HIS CYS PRO ASP VAL CYS PRO GLU
SEQRES 4 C 165 GLU LEU GLU LYS MSE ILE GLN VAL VAL ASP GLU ILE ASP
SEQRES 5 C 165 SER ILE THR THR LEU PRO ASP LEU THR PRO LEU PHE ILE
SEQRES 6 C 165 SER ILE ASP PRO GLU ARG ASP THR LYS GLU ALA ILE ALA
SEQRES 7 C 165 ASN TYR VAL LYS GLU PHE SER PRO LYS LEU VAL GLY LEU
SEQRES 8 C 165 THR GLY THR ARG GLU GLU VAL ASP GLN VAL ALA ARG ALA
SEQRES 9 C 165 TYR ARG VAL TYR TYR SER PRO GLY PRO LYS ASP GLU ASP
SEQRES 10 C 165 GLU ASP TYR ILE VAL ASP HIS THR ILE ILE MSE TYR LEU
SEQRES 11 C 165 ILE GLY PRO ASP GLY GLU PHE LEU ASP TYR PHE GLY GLN
SEQRES 12 C 165 ASN LYS ARG LYS GLY GLU ILE ALA ALA SER ILE ALA THR
SEQRES 13 C 165 HIS MSE ARG PRO TYR ARG LYS LYS SER
MODRES 1WP0 MSE A 180 MET SELENOMETHIONINE
MODRES 1WP0 MSE A 264 MET SELENOMETHIONINE
MODRES 1WP0 MSE A 294 MET SELENOMETHIONINE
MODRES 1WP0 MSE B 137 MET SELENOMETHIONINE
MODRES 1WP0 MSE B 180 MET SELENOMETHIONINE
MODRES 1WP0 MSE B 264 MET SELENOMETHIONINE
MODRES 1WP0 MSE B 294 MET SELENOMETHIONINE
MODRES 1WP0 MSE C 137 MET SELENOMETHIONINE
MODRES 1WP0 MSE C 180 MET SELENOMETHIONINE
MODRES 1WP0 MSE C 264 MET SELENOMETHIONINE
MODRES 1WP0 MSE C 294 MET SELENOMETHIONINE
HET MSE A 180 8
HET MSE A 264 8
HET MSE A 294 8
HET MSE B 137 8
HET MSE B 180 8
HET MSE B 264 8
HET MSE B 294 8
HET MSE C 137 8
HET MSE C 180 8
HET MSE C 264 8
HET MSE C 294 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 11(C5 H11 N O2 SE)
FORMUL 4 HOH *26(H2 O)
HELIX 1 1 LYS A 153 LEU A 156 5 4
HELIX 2 2 ASP A 171 ILE A 190 1 20
HELIX 3 3 THR A 209 GLU A 219 1 11
HELIX 4 4 THR A 230 TYR A 241 1 12
HELIX 5 5 ASP A 251 ASP A 255 5 5
HELIX 6 6 ARG A 282 ARG A 295 1 14
HELIX 7 7 LYS B 153 LEU B 156 5 4
HELIX 8 8 ASP B 171 ILE B 190 1 20
HELIX 9 9 THR B 209 GLU B 219 1 11
HELIX 10 10 THR B 230 TYR B 241 1 12
HELIX 11 11 ARG B 282 ARG B 295 1 14
HELIX 12 12 LYS C 153 LEU C 156 5 4
HELIX 13 13 ASP C 171 ILE C 190 1 20
HELIX 14 14 THR C 209 SER C 221 1 13
HELIX 15 15 THR C 230 TYR C 241 1 12
HELIX 16 16 ARG C 282 ARG C 295 1 14
SHEET 1 A 7 ARG A 149 THR A 151 0
SHEET 2 A 7 SER A 141 THR A 144 -1 N LEU A 142 O LYS A 150
SHEET 3 A 7 VAL A 225 THR A 228 -1 O THR A 228 N THR A 143
SHEET 4 A 7 LEU A 196 SER A 202 1 N PHE A 200 O LEU A 227
SHEET 5 A 7 TRP A 159 GLY A 165 1 N TRP A 159 O THR A 197
SHEET 6 A 7 ILE A 263 ILE A 267 -1 O ILE A 267 N LEU A 160
SHEET 7 A 7 PHE A 273 GLY A 278 -1 O ASP A 275 N LEU A 266
SHEET 1 B 2 TYR A 245 PRO A 247 0
SHEET 2 B 2 VAL A 258 HIS A 260 -1 O ASP A 259 N SER A 246
SHEET 1 C 7 ARG B 149 THR B 151 0
SHEET 2 C 7 SER B 141 THR B 144 -1 N LEU B 142 O LYS B 150
SHEET 3 C 7 VAL B 225 THR B 228 -1 O THR B 228 N THR B 143
SHEET 4 C 7 THR B 197 SER B 202 1 N SER B 202 O LEU B 227
SHEET 5 C 7 LEU B 160 GLY B 165 1 N TYR B 163 O ILE B 201
SHEET 6 C 7 MSE B 264 ILE B 267 -1 O TYR B 265 N ILE B 162
SHEET 7 C 7 PHE B 273 PHE B 277 -1 O LEU B 274 N LEU B 266
SHEET 1 D 2 TYR B 245 PRO B 247 0
SHEET 2 D 2 VAL B 258 HIS B 260 -1 O ASP B 259 N SER B 246
SHEET 1 E 7 ARG C 149 THR C 151 0
SHEET 2 E 7 SER C 141 THR C 144 -1 N LEU C 142 O LYS C 150
SHEET 3 E 7 VAL C 225 THR C 228 -1 O THR C 228 N THR C 143
SHEET 4 E 7 LEU C 196 SER C 202 1 N PHE C 200 O VAL C 225
SHEET 5 E 7 TRP C 159 GLY C 165 1 N TRP C 159 O THR C 197
SHEET 6 E 7 ILE C 263 ILE C 267 -1 O TYR C 265 N ILE C 162
SHEET 7 E 7 PHE C 273 GLY C 278 -1 O ASP C 275 N LEU C 266
SHEET 1 F 2 TYR C 245 PRO C 247 0
SHEET 2 F 2 VAL C 258 HIS C 260 -1 O ASP C 259 N SER C 246
LINK C LYS A 179 N MSE A 180 1555 1555 1.33
LINK C MSE A 180 N ILE A 181 1555 1555 1.33
LINK C ILE A 263 N MSE A 264 1555 1555 1.33
LINK C MSE A 264 N TYR A 265 1555 1555 1.33
LINK C HIS A 293 N MSE A 294 1555 1555 1.33
LINK C MSE A 294 N ARG A 295 1555 1555 1.33
LINK C MSE B 137 N GLY B 138 1555 1555 1.33
LINK C LYS B 179 N MSE B 180 1555 1555 1.33
LINK C MSE B 180 N ILE B 181 1555 1555 1.33
LINK C ILE B 263 N MSE B 264 1555 1555 1.33
LINK C MSE B 264 N TYR B 265 1555 1555 1.33
LINK C HIS B 293 N MSE B 294 1555 1555 1.33
LINK C MSE B 294 N ARG B 295 1555 1555 1.33
LINK C MSE C 137 N GLY C 138 1555 1555 1.33
LINK C LYS C 179 N MSE C 180 1555 1555 1.33
LINK C MSE C 180 N ILE C 181 1555 1555 1.33
LINK C ILE C 263 N MSE C 264 1555 1555 1.33
LINK C MSE C 264 N TYR C 265 1555 1555 1.33
LINK C HIS C 293 N MSE C 294 1555 1555 1.33
LINK C MSE C 294 N ARG C 295 1555 1555 1.33
CRYST1 60.210 103.154 103.168 90.00 90.00 90.00 P 21 21 21 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 0.016609 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009694 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009693 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
