HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-MAR-07 2P5I
TITLE CRYSTAL STRUCTURE OF PROTEIN BH3822 FROM BACILLUS HALODURANS, A MEMBER
TITLE 2 OF THE BIOTIN/LIPOATE A/B PROTEIN LIGASE FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BH3822 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS C-125;
SOURCE 3 ORGANISM_TAXID: 272558;
SOURCE 4 STRAIN: C-125, DSM 18197, FERM 7344, JCM 9153;
SOURCE 5 ATCC: BAA-125;
SOURCE 6 GENE: BH3822;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PSGX3
KEYWDS PFAM03099, 10425B, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK STRUCTURAL GENOMIX RESEARCH CONSORTIUM,
KEYWDS 3 NYSGXRC, UNKNOWN FUNCTION, NEW YORK SGX RESEARCH CENTER FOR
KEYWDS 4 STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SUGADEV,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 3 03-FEB-21 2P5I 1 AUTHOR JRNL SEQADV LINK
REVDAT 2 24-FEB-09 2P5I 1 VERSN
REVDAT 1 27-MAR-07 2P5I 0
JRNL AUTH R.SUGADEV,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN FROM BACILLUS
JRNL TITL 2 HALODURANS: PFAM-PF03099
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.21 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 82501.290
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 16552
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) : 0.228
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.900
REMARK 3 FREE R VALUE TEST SET COUNT : 984
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2209
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2049
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.16000
REMARK 3 B22 (A**2) : 1.16000
REMARK 3 B33 (A**2) : -2.31000
REMARK 3 B12 (A**2) : 4.35000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.23
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : 1.260 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.290 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 42.39
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 : DNA-RNA_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 2 : DNA-RNA.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: THE MISSING RESIDUES ARE DUE TO LACK OF
REMARK 3 ELECTRON DENSITY
REMARK 4
REMARK 4 2P5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17318
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 19.90
REMARK 200 R MERGE (I) : 0.16500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 0.63100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 20% PEG 10000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 52.58533
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 26.29267
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 39.43900
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 13.14633
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 65.73167
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: 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 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 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LEU A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 GLN A 8
REMARK 465 GLN A 9
REMARK 465 HIS A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 GLN A 13
REMARK 465 ASP A 135
REMARK 465 HIS A 136
REMARK 465 ARG A 137
REMARK 465 ALA A 279
REMARK 465 GLU A 280
REMARK 465 GLU A 281
REMARK 465 GLY A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 HIS A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
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 25 0.03 -60.29
REMARK 500 ASN A 59 90.50 0.12
REMARK 500 LEU A 95 152.38 165.30
REMARK 500 ALA A 96 127.54 -38.15
REMARK 500 LEU A 277 -18.92 -39.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-10425B RELATED DB: TARGETDB
DBREF 2P5I A 4 280 UNP Q9K6A7 Q9K6A7_BACHD 2 278
SEQADV 2P5I MSE A 1 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I SER A 2 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I LEU A 3 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I MSE A 125 UNP Q9K6A7 MET 123 MODIFIED RESIDUE
SEQADV 2P5I MSE A 132 UNP Q9K6A7 MET 130 MODIFIED RESIDUE
SEQADV 2P5I MSE A 193 UNP Q9K6A7 MET 191 MODIFIED RESIDUE
SEQADV 2P5I MSE A 219 UNP Q9K6A7 MET 217 MODIFIED RESIDUE
SEQADV 2P5I MSE A 241 UNP Q9K6A7 MET 239 MODIFIED RESIDUE
SEQADV 2P5I GLU A 281 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I GLY A 282 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I HIS A 283 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I HIS A 284 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I HIS A 285 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I HIS A 286 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I HIS A 287 UNP Q9K6A7 CLONING ARTIFACT
SEQADV 2P5I HIS A 288 UNP Q9K6A7 CLONING ARTIFACT
SEQRES 1 A 288 MSE SER LEU SER LEU LEU LEU GLN GLN HIS LEU SER GLN
SEQRES 2 A 288 PRO TRP ARG PHE LEU ASP HIS THR SER PHE GLY PRO THR
SEQRES 3 A 288 PHE GLN ALA LEU GLN SER PHE ALA TYR ASP ASP THR LEU
SEQRES 4 A 288 CYS THR SER ILE GLY LYS SER GLN SER PRO PRO THR LEU
SEQRES 5 A 288 ARG ALA TRP VAL HIS HIS ASN THR VAL VAL LEU GLY ILE
SEQRES 6 A 288 GLN ASP SER ARG LEU PRO GLN ILE LYS ALA GLY ILE GLU
SEQRES 7 A 288 ALA LEU LYS GLY PHE GLN HIS ASP VAL ILE VAL ARG ASN
SEQRES 8 A 288 SER GLY GLY LEU ALA VAL VAL LEU ASP SER GLY ILE LEU
SEQRES 9 A 288 ASN LEU SER LEU VAL LEU LYS GLU GLU LYS GLY PHE SER
SEQRES 10 A 288 ILE ASP ASP GLY TYR GLU LEU MSE TYR GLU LEU ILE CYS
SEQRES 11 A 288 SER MSE PHE GLN ASP HIS ARG GLU GLN ILE GLU ALA ARG
SEQRES 12 A 288 GLU ILE VAL GLY SER TYR CYS PRO GLY SER TYR ASP LEU
SEQRES 13 A 288 SER ILE ASP GLY LYS LYS PHE ALA GLY ILE SER GLN ARG
SEQRES 14 A 288 ARG ILE ARG GLY GLY VAL ALA VAL GLN ILE TYR LEU CYS
SEQRES 15 A 288 VAL SER GLY SER GLY ALA GLU ARG ALA LYS MSE ILE ARG
SEQRES 16 A 288 THR PHE TYR ASP LYS ALA VAL ALA GLY GLN PRO THR LYS
SEQRES 17 A 288 PHE VAL TYR PRO ARG ILE LYS PRO GLU THR MSE ALA SER
SEQRES 18 A 288 LEU SER GLU LEU LEU GLY GLN PRO HIS ASN VAL SER ASP
SEQRES 19 A 288 VAL LEU LEU LYS ALA LEU MSE THR LEU GLN GLN HIS GLY
SEQRES 20 A 288 ALA SER LEU LEU THR GLU SER LEU SER ALA ASP GLU TRP
SEQRES 21 A 288 LEU LEU TYR GLU GLN HIS PHE ALA ARG ILE SER GLU ARG
SEQRES 22 A 288 ASN GLU LYS LEU LEU ALA GLU GLU GLY HIS HIS HIS HIS
SEQRES 23 A 288 HIS HIS
MODRES 2P5I MSE A 125 MET SELENOMETHIONINE
MODRES 2P5I MSE A 132 MET SELENOMETHIONINE
MODRES 2P5I MSE A 193 MET SELENOMETHIONINE
MODRES 2P5I MSE A 219 MET SELENOMETHIONINE
MODRES 2P5I MSE A 241 MET SELENOMETHIONINE
HET MSE A 125 8
HET MSE A 132 8
HET MSE A 193 8
HET MSE A 219 8
HET MSE A 241 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 HOH *93(H2 O)
HELIX 1 1 GLN A 28 GLY A 44 1 17
HELIX 2 2 ILE A 65 ARG A 69 1 5
HELIX 3 3 GLN A 72 PHE A 83 1 12
HELIX 4 4 SER A 117 PHE A 133 1 17
HELIX 5 5 SER A 186 ALA A 203 1 18
HELIX 6 6 LYS A 215 MSE A 219 5 5
HELIX 7 7 SER A 221 GLY A 227 1 7
HELIX 8 8 ASN A 231 HIS A 246 1 16
HELIX 9 9 SER A 256 LEU A 278 1 23
SHEET 1 A 8 GLU A 141 ALA A 142 0
SHEET 2 A 8 LEU A 156 ILE A 158 -1 O SER A 157 N GLU A 141
SHEET 3 A 8 LYS A 161 ILE A 171 -1 O LYS A 161 N ILE A 158
SHEET 4 A 8 GLY A 174 CYS A 182 -1 O CYS A 182 N PHE A 163
SHEET 5 A 8 ILE A 103 LYS A 111 -1 N LEU A 110 O VAL A 175
SHEET 6 A 8 THR A 51 TRP A 55 -1 N THR A 51 O VAL A 109
SHEET 7 A 8 ARG A 16 HIS A 20 1 N HIS A 20 O ALA A 54
SHEET 8 A 8 LEU A 251 THR A 252 1 O LEU A 251 N PHE A 17
SHEET 1 B 3 ASP A 86 ARG A 90 0
SHEET 2 B 3 THR A 60 GLY A 64 1 N LEU A 63 O ILE A 88
SHEET 3 B 3 VAL A 97 LEU A 99 -1 O LEU A 99 N THR A 60
LINK C LEU A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N TYR A 126 1555 1555 1.33
LINK C SER A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N PHE A 133 1555 1555 1.33
LINK C LYS A 192 N MSE A 193 1555 1555 1.33
LINK C MSE A 193 N ILE A 194 1555 1555 1.33
LINK C THR A 218 N MSE A 219 1555 1555 1.33
LINK C MSE A 219 N ALA A 220 1555 1555 1.33
LINK C LEU A 240 N MSE A 241 1555 1555 1.33
LINK C MSE A 241 N THR A 242 1555 1555 1.33
CRYST1 87.715 87.715 78.878 90.00 90.00 120.00 P 65 6
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 0.011401 0.006582 0.000000 0.00000
SCALE2 0.000000 0.013164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012678 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
