HEADER TRANSFERASE 16-OCT-02 1O6U
TITLE THE CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEC14-LIKE PROTEIN 2;
COMPND 3 CHAIN: A, C, E;
COMPND 4 SYNONYM: SUPERNATANT PROTEIN FACTOR;
COMPND 5 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: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28
KEYWDS LIPID TRANSFER, CRAL_TRIO, LIPID BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.STOCKER,C.SCHULZE-BRIESE,T.TOMIZAKI
REVDAT 2 24-FEB-09 1O6U 1 VERSN
REVDAT 1 17-OCT-03 1O6U 0
JRNL AUTH A.STOCKER,T.TOMIZAKI,C.SCHULZE-BRIESE,U.BAUMANN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN SUPERNATANT PROTEIN
JRNL TITL 2 FACTOR
JRNL REF STRUCTURE V. 10 1533 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12429094
JRNL DOI 10.1016/S0969-2126(02)00884-5
REMARK 2
REMARK 2 RESOLUTION. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1540738.85
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 175712
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) : 0.204
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.6
REMARK 3 FREE R VALUE TEST SET COUNT : 2754
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 20739
REMARK 3 BIN R VALUE (WORKING SET) : 0.269
REMARK 3 BIN FREE R VALUE : 0.306
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.7
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 355
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9264
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 294
REMARK 3 SOLVENT ATOMS : 647
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.90
REMARK 3 B22 (A**2) : -0.03
REMARK 3 B33 (A**2) : -3.87
REMARK 3 B12 (A**2) : 1.67
REMARK 3 B13 (A**2) : 0.19
REMARK 3 B23 (A**2) : 0.84
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.2
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.5
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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) : 1.7 ; 1.5
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.4 ; 2.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.3 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.0 ; 2.5
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MASK
REMARK 3 KSOL : 0.367266
REMARK 3 BSOL : 39.1085
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 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PLM_XPLOR_PAR.TXT
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : PLM_XPLOR_PAR.TXT
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT CARIIED OUT AGAINST PEAK
REMARK 3 ANOMALOUS DATA. SCATTERING FACTORS REFINED IN CNS: FP =-8.003;
REMARK 3 FDP=4.56
REMARK 4
REMARK 4 1O6U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-02.
REMARK 100 THE PDBE ID CODE IS EBI-11464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.30
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97884
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 184572
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.25100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 400
REMARK 400 COMPOUND
REMARK 400 CARRIER PROTEIN THAT BINDS TO SOME HYDROPHOBIC MOLECULES AND
REMARK 400 PROMOTES THEIR TRANSFER BETWEEN THE DIFFERENT CELLULAR SITES.
REMARK 400 BINDS WITH HIGH AFFINITY TO ALPHA-TOCOPHEROL. ALSO BINDS WITH A
REMARK 400 WEAKER AFFINITY TO OTHER TOCOPHEROLS AND TO TOCOTRIENOLS.
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 THR A 322
REMARK 465 LYS A 323
REMARK 465 MSE A 324
REMARK 465 GLY A 325
REMARK 465 ALA A 399
REMARK 465 GLY A 400
REMARK 465 THR A 401
REMARK 465 PRO A 402
REMARK 465 LYS A 403
REMARK 465 LYS C 323
REMARK 465 MSE C 324
REMARK 465 GLY C 325
REMARK 465 GLU C 326
REMARK 465 ARG C 327
REMARK 465 GLN C 328
REMARK 465 ARG C 329
REMARK 465 ALA C 330
REMARK 465 GLY C 331
REMARK 465 LEU C 397
REMARK 465 GLY C 398
REMARK 465 ALA C 399
REMARK 465 GLY C 400
REMARK 465 THR C 401
REMARK 465 PRO C 402
REMARK 465 LYS C 403
REMARK 465 GLY E 398
REMARK 465 ALA E 399
REMARK 465 GLY E 400
REMARK 465 THR E 401
REMARK 465 PRO E 402
REMARK 465 LYS E 403
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 GLY A 398 CA C O
REMARK 470 GLN C 396 CA C O CB CG CD OE1 NE2
REMARK 470 LYS E 323 CG CD CE NZ
REMARK 470 MSE E 324 CG SE CE
REMARK 470 LEU E 397 CA C O CB CG CD1 CD2
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 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 ASP A 7 45.81 -150.88
REMARK 500 ASN A 32 82.67 -153.73
REMARK 500 PRO A 33 48.63 -75.58
REMARK 500 GLU A 147 11.56 -140.09
REMARK 500 SER A 288 -165.24 -118.41
REMARK 500 ARG A 327 96.78 -68.74
REMARK 500 SER A 344 0.24 -68.64
REMARK 500 GLN A 396 -71.60 -72.63
REMARK 500 ASP C 7 55.71 -156.99
REMARK 500 GLU C 147 17.95 -148.89
REMARK 500 ALA C 312 -179.96 -174.62
REMARK 500 ASP E 7 59.19 -154.05
REMARK 500 GLU E 147 14.71 -146.55
REMARK 500 SER E 344 0.57 -66.23
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 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MSE E 324
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A1398
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM C1396
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM E1397
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OLM RELATED DB: PDB
REMARK 900 SUPERNATANT PROTEIN FACTOR IN COMPLEX WITH
REMARK 900 RRR-ALPHA-TOCOPHERYLQUINONE: A LINK BETWEEN
REMARK 900 OXIDIZED VITAMIN E AND CHOLESTEROL
REMARK 900 BIOSYNTHESIS
DBREF 1O6U A 1 403 UNP O76054 S142_HUMAN 1 403
DBREF 1O6U C 1 403 UNP O76054 S142_HUMAN 1 403
DBREF 1O6U E 1 403 UNP O76054 S142_HUMAN 1 403
SEQRES 1 A 403 MSE SER GLY ARG VAL GLY ASP LEU SER PRO ARG GLN LYS
SEQRES 2 A 403 GLU ALA LEU ALA LYS PHE ARG GLU ASN VAL GLN ASP VAL
SEQRES 3 A 403 LEU PRO ALA LEU PRO ASN PRO ASP ASP TYR PHE LEU LEU
SEQRES 4 A 403 ARG TRP LEU ARG ALA ARG SER PHE ASP LEU GLN LYS SER
SEQRES 5 A 403 GLU ALA MSE LEU ARG LYS HIS VAL GLU PHE ARG LYS GLN
SEQRES 6 A 403 LYS ASP ILE ASP ASN ILE ILE SER TRP GLN PRO PRO GLU
SEQRES 7 A 403 VAL ILE GLN GLN TYR LEU SER GLY GLY MSE CYS GLY TYR
SEQRES 8 A 403 ASP LEU ASP GLY CYS PRO VAL TRP TYR ASP ILE ILE GLY
SEQRES 9 A 403 PRO LEU ASP ALA LYS GLY LEU LEU PHE SER ALA SER LYS
SEQRES 10 A 403 GLN ASP LEU LEU ARG THR LYS MSE ARG GLU CYS GLU LEU
SEQRES 11 A 403 LEU LEU GLN GLU CYS ALA HIS GLN THR THR LYS LEU GLY
SEQRES 12 A 403 ARG LYS VAL GLU THR ILE THR ILE ILE TYR ASP CYS GLU
SEQRES 13 A 403 GLY LEU GLY LEU LYS HIS LEU TRP LYS PRO ALA VAL GLU
SEQRES 14 A 403 ALA TYR GLY GLU PHE LEU CYS MSE PHE GLU GLU ASN TYR
SEQRES 15 A 403 PRO GLU THR LEU LYS ARG LEU PHE VAL VAL LYS ALA PRO
SEQRES 16 A 403 LYS LEU PHE PRO VAL ALA TYR ASN LEU ILE LYS PRO PHE
SEQRES 17 A 403 LEU SER GLU ASP THR ARG LYS LYS ILE MSE VAL LEU GLY
SEQRES 18 A 403 ALA ASN TRP LYS GLU VAL LEU LEU LYS HIS ILE SER PRO
SEQRES 19 A 403 ASP GLN VAL PRO VAL GLU TYR GLY GLY THR MSE THR ASP
SEQRES 20 A 403 PRO ASP GLY ASN PRO LYS CYS LYS SER LYS ILE ASN TYR
SEQRES 21 A 403 GLY GLY ASP ILE PRO ARG LYS TYR TYR VAL ARG ASP GLN
SEQRES 22 A 403 VAL LYS GLN GLN TYR GLU HIS SER VAL GLN ILE SER ARG
SEQRES 23 A 403 GLY SER SER HIS GLN VAL GLU TYR GLU ILE LEU PHE PRO
SEQRES 24 A 403 GLY CYS VAL LEU ARG TRP GLN PHE MSE SER ASP GLY ALA
SEQRES 25 A 403 ASP VAL GLY PHE GLY ILE PHE LEU LYS THR LYS MSE GLY
SEQRES 26 A 403 GLU ARG GLN ARG ALA GLY GLU MSE THR GLU VAL LEU PRO
SEQRES 27 A 403 ASN GLN ARG TYR ASN SER HIS LEU VAL PRO GLU ASP GLY
SEQRES 28 A 403 THR LEU THR CYS SER ASP PRO GLY ILE TYR VAL LEU ARG
SEQRES 29 A 403 PHE ASP ASN THR TYR SER PHE ILE HIS ALA LYS LYS VAL
SEQRES 30 A 403 ASN PHE THR VAL GLU VAL LEU LEU PRO ASP LYS ALA SER
SEQRES 31 A 403 GLU GLU LYS MSE LYS GLN LEU GLY ALA GLY THR PRO LYS
SEQRES 1 C 403 MSE SER GLY ARG VAL GLY ASP LEU SER PRO ARG GLN LYS
SEQRES 2 C 403 GLU ALA LEU ALA LYS PHE ARG GLU ASN VAL GLN ASP VAL
SEQRES 3 C 403 LEU PRO ALA LEU PRO ASN PRO ASP ASP TYR PHE LEU LEU
SEQRES 4 C 403 ARG TRP LEU ARG ALA ARG SER PHE ASP LEU GLN LYS SER
SEQRES 5 C 403 GLU ALA MSE LEU ARG LYS HIS VAL GLU PHE ARG LYS GLN
SEQRES 6 C 403 LYS ASP ILE ASP ASN ILE ILE SER TRP GLN PRO PRO GLU
SEQRES 7 C 403 VAL ILE GLN GLN TYR LEU SER GLY GLY MSE CYS GLY TYR
SEQRES 8 C 403 ASP LEU ASP GLY CYS PRO VAL TRP TYR ASP ILE ILE GLY
SEQRES 9 C 403 PRO LEU ASP ALA LYS GLY LEU LEU PHE SER ALA SER LYS
SEQRES 10 C 403 GLN ASP LEU LEU ARG THR LYS MSE ARG GLU CYS GLU LEU
SEQRES 11 C 403 LEU LEU GLN GLU CYS ALA HIS GLN THR THR LYS LEU GLY
SEQRES 12 C 403 ARG LYS VAL GLU THR ILE THR ILE ILE TYR ASP CYS GLU
SEQRES 13 C 403 GLY LEU GLY LEU LYS HIS LEU TRP LYS PRO ALA VAL GLU
SEQRES 14 C 403 ALA TYR GLY GLU PHE LEU CYS MSE PHE GLU GLU ASN TYR
SEQRES 15 C 403 PRO GLU THR LEU LYS ARG LEU PHE VAL VAL LYS ALA PRO
SEQRES 16 C 403 LYS LEU PHE PRO VAL ALA TYR ASN LEU ILE LYS PRO PHE
SEQRES 17 C 403 LEU SER GLU ASP THR ARG LYS LYS ILE MSE VAL LEU GLY
SEQRES 18 C 403 ALA ASN TRP LYS GLU VAL LEU LEU LYS HIS ILE SER PRO
SEQRES 19 C 403 ASP GLN VAL PRO VAL GLU TYR GLY GLY THR MSE THR ASP
SEQRES 20 C 403 PRO ASP GLY ASN PRO LYS CYS LYS SER LYS ILE ASN TYR
SEQRES 21 C 403 GLY GLY ASP ILE PRO ARG LYS TYR TYR VAL ARG ASP GLN
SEQRES 22 C 403 VAL LYS GLN GLN TYR GLU HIS SER VAL GLN ILE SER ARG
SEQRES 23 C 403 GLY SER SER HIS GLN VAL GLU TYR GLU ILE LEU PHE PRO
SEQRES 24 C 403 GLY CYS VAL LEU ARG TRP GLN PHE MSE SER ASP GLY ALA
SEQRES 25 C 403 ASP VAL GLY PHE GLY ILE PHE LEU LYS THR LYS MSE GLY
SEQRES 26 C 403 GLU ARG GLN ARG ALA GLY GLU MSE THR GLU VAL LEU PRO
SEQRES 27 C 403 ASN GLN ARG TYR ASN SER HIS LEU VAL PRO GLU ASP GLY
SEQRES 28 C 403 THR LEU THR CYS SER ASP PRO GLY ILE TYR VAL LEU ARG
SEQRES 29 C 403 PHE ASP ASN THR TYR SER PHE ILE HIS ALA LYS LYS VAL
SEQRES 30 C 403 ASN PHE THR VAL GLU VAL LEU LEU PRO ASP LYS ALA SER
SEQRES 31 C 403 GLU GLU LYS MSE LYS GLN LEU GLY ALA GLY THR PRO LYS
SEQRES 1 E 403 MSE SER GLY ARG VAL GLY ASP LEU SER PRO ARG GLN LYS
SEQRES 2 E 403 GLU ALA LEU ALA LYS PHE ARG GLU ASN VAL GLN ASP VAL
SEQRES 3 E 403 LEU PRO ALA LEU PRO ASN PRO ASP ASP TYR PHE LEU LEU
SEQRES 4 E 403 ARG TRP LEU ARG ALA ARG SER PHE ASP LEU GLN LYS SER
SEQRES 5 E 403 GLU ALA MSE LEU ARG LYS HIS VAL GLU PHE ARG LYS GLN
SEQRES 6 E 403 LYS ASP ILE ASP ASN ILE ILE SER TRP GLN PRO PRO GLU
SEQRES 7 E 403 VAL ILE GLN GLN TYR LEU SER GLY GLY MSE CYS GLY TYR
SEQRES 8 E 403 ASP LEU ASP GLY CYS PRO VAL TRP TYR ASP ILE ILE GLY
SEQRES 9 E 403 PRO LEU ASP ALA LYS GLY LEU LEU PHE SER ALA SER LYS
SEQRES 10 E 403 GLN ASP LEU LEU ARG THR LYS MSE ARG GLU CYS GLU LEU
SEQRES 11 E 403 LEU LEU GLN GLU CYS ALA HIS GLN THR THR LYS LEU GLY
SEQRES 12 E 403 ARG LYS VAL GLU THR ILE THR ILE ILE TYR ASP CYS GLU
SEQRES 13 E 403 GLY LEU GLY LEU LYS HIS LEU TRP LYS PRO ALA VAL GLU
SEQRES 14 E 403 ALA TYR GLY GLU PHE LEU CYS MSE PHE GLU GLU ASN TYR
SEQRES 15 E 403 PRO GLU THR LEU LYS ARG LEU PHE VAL VAL LYS ALA PRO
SEQRES 16 E 403 LYS LEU PHE PRO VAL ALA TYR ASN LEU ILE LYS PRO PHE
SEQRES 17 E 403 LEU SER GLU ASP THR ARG LYS LYS ILE MSE VAL LEU GLY
SEQRES 18 E 403 ALA ASN TRP LYS GLU VAL LEU LEU LYS HIS ILE SER PRO
SEQRES 19 E 403 ASP GLN VAL PRO VAL GLU TYR GLY GLY THR MSE THR ASP
SEQRES 20 E 403 PRO ASP GLY ASN PRO LYS CYS LYS SER LYS ILE ASN TYR
SEQRES 21 E 403 GLY GLY ASP ILE PRO ARG LYS TYR TYR VAL ARG ASP GLN
SEQRES 22 E 403 VAL LYS GLN GLN TYR GLU HIS SER VAL GLN ILE SER ARG
SEQRES 23 E 403 GLY SER SER HIS GLN VAL GLU TYR GLU ILE LEU PHE PRO
SEQRES 24 E 403 GLY CYS VAL LEU ARG TRP GLN PHE MSE SER ASP GLY ALA
SEQRES 25 E 403 ASP VAL GLY PHE GLY ILE PHE LEU LYS THR LYS MSE GLY
SEQRES 26 E 403 GLU ARG GLN ARG ALA GLY GLU MSE THR GLU VAL LEU PRO
SEQRES 27 E 403 ASN GLN ARG TYR ASN SER HIS LEU VAL PRO GLU ASP GLY
SEQRES 28 E 403 THR LEU THR CYS SER ASP PRO GLY ILE TYR VAL LEU ARG
SEQRES 29 E 403 PHE ASP ASN THR TYR SER PHE ILE HIS ALA LYS LYS VAL
SEQRES 30 E 403 ASN PHE THR VAL GLU VAL LEU LEU PRO ASP LYS ALA SER
SEQRES 31 E 403 GLU GLU LYS MSE LYS GLN LEU GLY ALA GLY THR PRO LYS
MODRES 1O6U MSE A 1 MET SELENOMETHIONINE
MODRES 1O6U MSE A 55 MET SELENOMETHIONINE
MODRES 1O6U MSE A 88 MET SELENOMETHIONINE
MODRES 1O6U MSE A 125 MET SELENOMETHIONINE
MODRES 1O6U MSE A 177 MET SELENOMETHIONINE
MODRES 1O6U MSE A 218 MET SELENOMETHIONINE
MODRES 1O6U MSE A 245 MET SELENOMETHIONINE
MODRES 1O6U MSE A 308 MET SELENOMETHIONINE
MODRES 1O6U MSE A 333 MET SELENOMETHIONINE
MODRES 1O6U MSE A 394 MET SELENOMETHIONINE
MODRES 1O6U MSE C 1 MET SELENOMETHIONINE
MODRES 1O6U MSE C 55 MET SELENOMETHIONINE
MODRES 1O6U MSE C 88 MET SELENOMETHIONINE
MODRES 1O6U MSE C 125 MET SELENOMETHIONINE
MODRES 1O6U MSE C 177 MET SELENOMETHIONINE
MODRES 1O6U MSE C 218 MET SELENOMETHIONINE
MODRES 1O6U MSE C 245 MET SELENOMETHIONINE
MODRES 1O6U MSE C 308 MET SELENOMETHIONINE
MODRES 1O6U MSE C 333 MET SELENOMETHIONINE
MODRES 1O6U MSE C 394 MET SELENOMETHIONINE
MODRES 1O6U MSE E 1 MET SELENOMETHIONINE
MODRES 1O6U MSE E 55 MET SELENOMETHIONINE
MODRES 1O6U MSE E 88 MET SELENOMETHIONINE
MODRES 1O6U MSE E 125 MET SELENOMETHIONINE
MODRES 1O6U MSE E 177 MET SELENOMETHIONINE
MODRES 1O6U MSE E 218 MET SELENOMETHIONINE
MODRES 1O6U MSE E 245 MET SELENOMETHIONINE
MODRES 1O6U MSE E 308 MET SELENOMETHIONINE
MODRES 1O6U MSE E 324 MET SELENOMETHIONINE
MODRES 1O6U MSE E 333 MET SELENOMETHIONINE
MODRES 1O6U MSE E 394 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 55 8
HET MSE A 88 8
HET MSE A 125 8
HET MSE A 177 8
HET MSE A 218 8
HET MSE A 245 8
HET MSE A 308 8
HET MSE A 333 8
HET MSE A 394 8
HET MSE C 1 8
HET MSE C 55 8
HET MSE C 88 8
HET MSE C 125 8
HET MSE C 177 8
HET MSE C 218 8
HET MSE C 245 8
HET MSE C 308 8
HET MSE C 333 8
HET MSE C 394 8
HET MSE E 1 8
HET MSE E 55 8
HET MSE E 88 8
HET MSE E 125 8
HET MSE E 177 8
HET MSE E 218 8
HET MSE E 245 8
HET MSE E 308 8
HET MSE E 324 5
HET MSE E 333 8
HET MSE E 394 8
HET PLM A1398 18
HET PLM C1396 18
HET PLM E1397 18
HETNAM MSE SELENOMETHIONINE
HETNAM PLM PALMITIC ACID
FORMUL 1 MSE 31(C5 H11 N O2 SE)
FORMUL 4 PLM 3(C16 H32 O2)
FORMUL 7 HOH *647(H2 O1)
HELIX 1 1 SER A 9 VAL A 23 1 15
HELIX 2 2 GLN A 24 LEU A 30 5 7
HELIX 3 3 ASP A 34 ARG A 45 1 12
HELIX 4 4 ASP A 48 ASP A 67 1 20
HELIX 5 5 ILE A 68 TRP A 74 5 7
HELIX 6 6 PRO A 77 LEU A 84 1 8
HELIX 7 7 ASP A 107 ALA A 115 1 9
HELIX 8 8 SER A 116 GLY A 143 1 28
HELIX 9 9 GLY A 159 LEU A 163 5 5
HELIX 10 10 TRP A 164 TYR A 182 1 19
HELIX 11 11 LEU A 197 LYS A 206 1 10
HELIX 12 12 PRO A 207 LEU A 209 5 3
HELIX 13 13 SER A 210 LYS A 216 1 7
HELIX 14 14 ASN A 223 LEU A 229 1 7
HELIX 15 15 SER A 233 VAL A 237 5 5
HELIX 16 16 VAL A 239 GLY A 242 5 4
HELIX 17 17 PRO A 265 TYR A 269 5 5
HELIX 18 18 ARG A 329 MSE A 333 5 5
HELIX 19 19 ASP A 387 LEU A 397 1 11
HELIX 20 20 SER C 9 VAL C 23 1 15
HELIX 21 21 VAL C 26 LEU C 30 5 5
HELIX 22 22 ASP C 34 ARG C 45 1 12
HELIX 23 23 ASP C 48 LYS C 66 1 19
HELIX 24 24 ASP C 67 TRP C 74 5 8
HELIX 25 25 PRO C 77 LEU C 84 1 8
HELIX 26 26 ASP C 107 ALA C 115 1 9
HELIX 27 27 SER C 116 GLY C 143 1 28
HELIX 28 28 GLY C 159 LEU C 163 5 5
HELIX 29 29 TRP C 164 TYR C 182 1 19
HELIX 30 30 LEU C 197 LYS C 206 1 10
HELIX 31 31 PRO C 207 LEU C 209 5 3
HELIX 32 32 SER C 210 LYS C 216 1 7
HELIX 33 33 ASN C 223 LEU C 229 1 7
HELIX 34 34 SER C 233 VAL C 237 5 5
HELIX 35 35 VAL C 239 GLY C 242 5 4
HELIX 36 36 PRO C 265 TYR C 269 5 5
HELIX 37 37 ASP C 387 LYS C 395 1 9
HELIX 38 38 SER E 9 VAL E 23 1 15
HELIX 39 39 GLN E 24 LEU E 30 5 7
HELIX 40 40 ASP E 34 ARG E 45 1 12
HELIX 41 41 ASP E 48 LYS E 66 1 19
HELIX 42 42 ASP E 67 ILE E 71 5 5
HELIX 43 43 PRO E 77 LEU E 84 1 8
HELIX 44 44 ASP E 107 ALA E 115 1 9
HELIX 45 45 SER E 116 GLY E 143 1 28
HELIX 46 46 GLY E 159 LEU E 163 5 5
HELIX 47 47 TRP E 164 TYR E 182 1 19
HELIX 48 48 LEU E 197 LYS E 206 1 10
HELIX 49 49 PRO E 207 LEU E 209 5 3
HELIX 50 50 SER E 210 LYS E 216 1 7
HELIX 51 51 ASN E 223 LEU E 229 1 7
HELIX 52 52 SER E 233 VAL E 237 5 5
HELIX 53 53 VAL E 239 GLY E 242 5 4
HELIX 54 54 PRO E 265 TYR E 269 5 5
HELIX 55 55 ASP E 387 GLN E 396 1 10
SHEET 1 AA 5 GLY A 87 TYR A 91 0
SHEET 2 AA 5 PRO A 97 ILE A 102 -1 O VAL A 98 N CYS A 89
SHEET 3 AA 5 ILE A 149 ASP A 154 1 O THR A 150 N TRP A 99
SHEET 4 AA 5 LEU A 186 VAL A 192 1 N LYS A 187 O ILE A 149
SHEET 5 AA 5 ILE A 217 VAL A 219 1 O MSE A 218 N VAL A 191
SHEET 1 AB 4 HIS A 280 ILE A 284 0
SHEET 2 AB 4 LYS A 375 LEU A 384 -1 O LYS A 375 N ILE A 284
SHEET 3 AB 4 CYS A 301 SER A 309 -1 O VAL A 302 N LEU A 384
SHEET 4 AB 4 GLU A 349 CYS A 355 -1 O GLU A 349 N PHE A 307
SHEET 1 AC 4 SER A 289 ILE A 296 0
SHEET 2 AC 4 GLY A 359 ASP A 366 -1 O GLY A 359 N ILE A 296
SHEET 3 AC 4 VAL A 314 LEU A 320 -1 O GLY A 315 N ASP A 366
SHEET 4 AC 4 THR A 334 TYR A 342 -1 O THR A 334 N LEU A 320
SHEET 1 CA 5 GLY C 87 TYR C 91 0
SHEET 2 CA 5 PRO C 97 ILE C 102 -1 O VAL C 98 N CYS C 89
SHEET 3 CA 5 ILE C 149 ASP C 154 1 O THR C 150 N TRP C 99
SHEET 4 CA 5 LEU C 186 VAL C 192 1 N LYS C 187 O ILE C 149
SHEET 5 CA 5 ILE C 217 VAL C 219 1 O MSE C 218 N VAL C 191
SHEET 1 CB 4 HIS C 280 GLN C 283 0
SHEET 2 CB 4 LYS C 376 LEU C 384 -1 O VAL C 377 N VAL C 282
SHEET 3 CB 4 VAL C 302 ASP C 310 -1 O VAL C 302 N LEU C 384
SHEET 4 CB 4 GLU C 349 THR C 354 -1 O GLU C 349 N PHE C 307
SHEET 1 CC 4 SER C 289 ILE C 296 0
SHEET 2 CC 4 GLY C 359 ASP C 366 -1 O GLY C 359 N ILE C 296
SHEET 3 CC 4 VAL C 314 LYS C 321 -1 O GLY C 315 N ASP C 366
SHEET 4 CC 4 MSE C 333 TYR C 342 -1 O THR C 334 N LEU C 320
SHEET 1 EA 5 GLY E 87 TYR E 91 0
SHEET 2 EA 5 PRO E 97 ILE E 102 -1 O VAL E 98 N CYS E 89
SHEET 3 EA 5 ILE E 149 ASP E 154 1 O THR E 150 N TRP E 99
SHEET 4 EA 5 LEU E 186 VAL E 192 1 N LYS E 187 O ILE E 149
SHEET 5 EA 5 ILE E 217 VAL E 219 1 O MSE E 218 N VAL E 191
SHEET 1 EB 4 HIS E 280 ILE E 284 0
SHEET 2 EB 4 LYS E 375 LEU E 384 -1 O LYS E 375 N ILE E 284
SHEET 3 EB 4 CYS E 301 SER E 309 -1 O VAL E 302 N LEU E 384
SHEET 4 EB 4 GLU E 349 CYS E 355 -1 O GLU E 349 N PHE E 307
SHEET 1 EC 4 SER E 289 ILE E 296 0
SHEET 2 EC 4 GLY E 359 ASP E 366 -1 O GLY E 359 N ILE E 296
SHEET 3 EC 4 VAL E 314 LEU E 320 -1 O GLY E 315 N ASP E 366
SHEET 4 EC 4 THR E 334 TYR E 342 -1 O THR E 334 N LEU E 320
LINK C MSE A 1 N SER A 2 1555 1555 1.33
LINK C ALA A 54 N MSE A 55 1555 1555 1.33
LINK C MSE A 55 N LEU A 56 1555 1555 1.33
LINK C GLY A 87 N MSE A 88 1555 1555 1.32
LINK C MSE A 88 N CYS A 89 1555 1555 1.32
LINK C LYS A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N ARG A 126 1555 1555 1.33
LINK C CYS A 176 N MSE A 177 1555 1555 1.33
LINK C MSE A 177 N PHE A 178 1555 1555 1.33
LINK C ILE A 217 N MSE A 218 1555 1555 1.33
LINK C MSE A 218 N VAL A 219 1555 1555 1.33
LINK C THR A 244 N MSE A 245 1555 1555 1.33
LINK C MSE A 245 N THR A 246 1555 1555 1.33
LINK C PHE A 307 N MSE A 308 1555 1555 1.33
LINK C MSE A 308 N SER A 309 1555 1555 1.32
LINK C GLU A 332 N MSE A 333 1555 1555 1.33
LINK C MSE A 333 N THR A 334 1555 1555 1.33
LINK C LYS A 393 N MSE A 394 1555 1555 1.33
LINK C MSE A 394 N LYS A 395 1555 1555 1.33
LINK C MSE C 1 N SER C 2 1555 1555 1.33
LINK C ALA C 54 N MSE C 55 1555 1555 1.33
LINK C MSE C 55 N LEU C 56 1555 1555 1.33
LINK C GLY C 87 N MSE C 88 1555 1555 1.33
LINK C MSE C 88 N CYS C 89 1555 1555 1.33
LINK C LYS C 124 N MSE C 125 1555 1555 1.33
LINK C MSE C 125 N ARG C 126 1555 1555 1.32
LINK C CYS C 176 N MSE C 177 1555 1555 1.33
LINK C MSE C 177 N PHE C 178 1555 1555 1.33
LINK C ILE C 217 N MSE C 218 1555 1555 1.33
LINK C MSE C 218 N VAL C 219 1555 1555 1.33
LINK C THR C 244 N MSE C 245 1555 1555 1.33
LINK C MSE C 245 N THR C 246 1555 1555 1.33
LINK C PHE C 307 N MSE C 308 1555 1555 1.32
LINK C MSE C 308 N SER C 309 1555 1555 1.33
LINK C GLU C 332 N MSE C 333 1555 1555 1.33
LINK C MSE C 333 N THR C 334 1555 1555 1.33
LINK C LYS C 393 N MSE C 394 1555 1555 1.33
LINK C MSE C 394 N LYS C 395 1555 1555 1.33
LINK C MSE E 1 N SER E 2 1555 1555 1.33
LINK C ALA E 54 N MSE E 55 1555 1555 1.33
LINK C MSE E 55 N LEU E 56 1555 1555 1.33
LINK C GLY E 87 N MSE E 88 1555 1555 1.33
LINK C MSE E 88 N CYS E 89 1555 1555 1.33
LINK C LYS E 124 N MSE E 125 1555 1555 1.33
LINK C MSE E 125 N ARG E 126 1555 1555 1.33
LINK C CYS E 176 N MSE E 177 1555 1555 1.33
LINK C MSE E 177 N PHE E 178 1555 1555 1.33
LINK C ILE E 217 N MSE E 218 1555 1555 1.33
LINK C MSE E 218 N VAL E 219 1555 1555 1.33
LINK C THR E 244 N MSE E 245 1555 1555 1.33
LINK C MSE E 245 N THR E 246 1555 1555 1.33
LINK C PHE E 307 N MSE E 308 1555 1555 1.32
LINK C MSE E 308 N SER E 309 1555 1555 1.33
LINK C LYS E 323 N MSE E 324 1555 1555 1.33
LINK C MSE E 324 N GLY E 325 1555 1555 1.33
LINK C GLU E 332 N MSE E 333 1555 1555 1.33
LINK C MSE E 333 N THR E 334 1555 1555 1.33
LINK C LYS E 393 N MSE E 394 1555 1555 1.33
LINK C MSE E 394 N LYS E 395 1555 1555 1.33
SITE 1 AC1 5 TYR A 153 HIS A 162 LEU A 175 LEU A 189
SITE 2 AC1 5 ALA A 201
SITE 1 AC2 5 TYR C 153 HIS C 162 LEU C 189 ALA C 201
SITE 2 AC2 5 TYR C 202
SITE 1 AC3 6 ILE E 151 TYR E 153 LEU E 175 LEU E 189
SITE 2 AC3 6 PHE E 198 ILE E 205
CRYST1 59.794 84.240 87.111 116.26 102.39 99.87 P 1 3
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 0.016724 0.002910 0.005908 0.00000
SCALE2 0.000000 0.012049 0.006920 0.00000
SCALE3 0.000000 0.000000 0.013554 0.00000
HETATM 1 N MSE A 1 -4.895 -10.371 19.086 1.00 48.28 N
HETATM 2 CA MSE A 1 -5.373 -9.567 17.925 1.00 47.98 C
HETATM 3 C MSE A 1 -5.741 -8.151 18.370 1.00 45.97 C
HETATM 4 O MSE A 1 -5.934 -7.903 19.561 1.00 48.18 O
HETATM 5 CB MSE A 1 -6.577 -10.258 17.279 1.00 52.01 C
HETATM 6 CG MSE A 1 -6.284 -11.669 16.774 1.00 54.17 C
HETATM 7 SE MSE A 1 -5.050 -11.738 15.271 1.00 62.63 SE
HETATM 8 CE MSE A 1 -3.376 -11.723 16.243 1.00 58.96 C
(ATOM LINES ARE NOT SHOWN.)
END