HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-03 1UFA
TITLE CRYSTAL STRUCTURE OF TT1467 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TT1467 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.IDAKA,T.TERADA,K.MURAYAMA,H.YAMAGUCHI,O.NUREKI,R.ISHITANI,
AUTHOR 2 S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 27-DEC-23 1UFA 1 LINK
REVDAT 3 04-OCT-17 1UFA 1 REMARK
REVDAT 2 24-FEB-09 1UFA 1 VERSN
REVDAT 1 28-NOV-03 1UFA 0
JRNL AUTH M.IDAKA,T.TERADA,K.MURAYAMA,H.YAMAGUCHI,O.NUREKI,R.ISHITANI,
JRNL AUTH 2 S.KURAMITSU,M.SHIROUZU,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF TT1467 FROM THERMUS THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2401211.320
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27591
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) : 0.187
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2753
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4035
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 457
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4116
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.26000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 39.74
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UFA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000005761.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-03
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 : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 8.000
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) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.1
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: SHARP, AUTOSHARP, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, SODIUM HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 59.68800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 59.68800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.94900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 59.68800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 59.68800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.94900
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 59.68800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.68800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.94900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 59.68800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.68800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 36.94900
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: 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 PRO A 235
REMARK 465 TYR A 236
REMARK 465 GLY A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 ALA A 240
REMARK 465 LEU A 241
REMARK 465 GLY A 242
REMARK 465 ARG A 518
REMARK 465 GLU A 519
REMARK 465 ALA A 520
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 ALA A 53 73.60 -153.30
REMARK 500 THR A 141 -168.07 -109.28
REMARK 500 MSE A 185 29.00 47.16
REMARK 500 THR A 304 -57.73 71.10
REMARK 500 ALA A 308 141.53 -34.04
REMARK 500 ASP A 409 -137.40 -129.41
REMARK 500 ASN A 415 -178.29 -170.18
REMARK 500 ALA A 470 63.54 178.89
REMARK 500 PHE A 507 68.53 66.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003001467.1 RELATED DB: TARGETDB
DBREF 1UFA A 1 520 UNP P84162 P84162_THETH 1 520
SEQRES 1 A 520 MSE ALA ARG PHE ALA LEU VAL LEU HIS ALA HIS LEU PRO
SEQRES 2 A 520 TYR VAL ARG ALA HIS GLY MSE TRP PRO PHE GLY GLU GLU
SEQRES 3 A 520 THR LEU TYR GLU ALA MSE ALA GLU THR TYR LEU PRO LEU
SEQRES 4 A 520 ILE ARG VAL LEU GLU ARG LEU ARG ALA GLU GLY VAL GLU
SEQRES 5 A 520 ALA PRO PHE THR LEU GLY ILE THR PRO ILE LEU ALA GLU
SEQRES 6 A 520 GLN LEU ALA ASP ALA ARG ILE LYS GLU GLY PHE TRP ALA
SEQRES 7 A 520 TYR ALA LYS ASP ARG LEU GLU ARG ALA GLN GLY ASP TYR
SEQRES 8 A 520 GLN ARG TYR ARG GLY THR ALA LEU GLU ALA SER ALA ARG
SEQRES 9 A 520 HIS GLN VAL ALA PHE TRP GLU LEU THR LEU ASP HIS PHE
SEQRES 10 A 520 GLN ARG LEU SER GLY ASP LEU VAL ALA ALA PHE ARG LYS
SEQRES 11 A 520 ALA GLU GLU GLY GLY GLN VAL GLU LEU ILE THR SER ASN
SEQRES 12 A 520 ALA THR HIS GLY TYR SER PRO LEU LEU GLY TYR ASP GLU
SEQRES 13 A 520 ALA LEU TRP ALA GLN ILE LYS THR GLY VAL SER THR TYR
SEQRES 14 A 520 ARG ARG HIS PHE ALA LYS ASP PRO THR GLY PHE TRP LEU
SEQRES 15 A 520 PRO GLU MSE ALA TYR ARG PRO LYS GLY PRO TRP LYS PRO
SEQRES 16 A 520 PRO VAL GLU GLY PRO PRO GLU GLY VAL ARG PRO GLY VAL
SEQRES 17 A 520 ASP GLU LEU LEU MSE ARG ALA GLY ILE ARG TYR THR PHE
SEQRES 18 A 520 VAL ASP ALA HIS LEU VAL GLN GLY GLY GLU PRO LEU SER
SEQRES 19 A 520 PRO TYR GLY GLU ALA ALA LEU GLY PRO VAL GLU SER GLN
SEQRES 20 A 520 GLU ALA THR TYR HIS VAL HIS GLU LEU GLU SER GLY LEU
SEQRES 21 A 520 ARG VAL LEU ALA ARG ASN PRO GLU THR THR LEU GLN VAL
SEQRES 22 A 520 TRP SER ALA ASP TYR GLY TYR PRO GLY GLU GLY LEU TYR
SEQRES 23 A 520 ARG GLU PHE HIS ARG LYS ASP PRO LEU SER GLY LEU HIS
SEQRES 24 A 520 HIS TRP ARG VAL THR HIS ARG LYS ALA ASP LEU ALA GLU
SEQRES 25 A 520 LYS ALA PRO TYR ASP PRO GLU ALA ALA PHE ALA LYS THR
SEQRES 26 A 520 GLU GLU HIS ALA ARG HIS PHE VAL GLY LEU LEU GLU ARG
SEQRES 27 A 520 LEU ALA GLY ARG HIS PRO GLU GLY VAL ILE LEU SER PRO
SEQRES 28 A 520 TYR ASP ALA GLU LEU PHE GLY HIS TRP TRP TYR GLU GLY
SEQRES 29 A 520 VAL ALA TRP LEU GLU ALA VAL LEU ARG LEU LEU ALA GLN
SEQRES 30 A 520 ASN PRO LYS VAL ARG PRO VAL THR ALA ARG GLU ALA VAL
SEQRES 31 A 520 GLN GLY PRO ALA VAL ARG THR ALA LEU PRO GLU GLY SER
SEQRES 32 A 520 TRP GLY ARG GLY GLY ASP HIS ARG VAL TRP LEU ASN GLU
SEQRES 33 A 520 LYS THR LEU ASP TYR TRP GLU LYS VAL TYR ARG ALA GLU
SEQRES 34 A 520 GLY ALA MSE ARG GLU ALA ALA ARG ARG GLY VAL LEU PRO
SEQRES 35 A 520 GLU GLY VAL LEU ARG GLN ALA MSE ARG GLU LEU LEU LEU
SEQRES 36 A 520 LEU GLU ALA SER ASP TRP PRO PHE LEU MSE GLU THR GLY
SEQRES 37 A 520 GLN ALA GLU ALA TYR ALA ARG GLU ARG TYR GLU GLU HIS
SEQRES 38 A 520 ALA ARG ALA PHE PHE HIS LEU LEU LYS GLY ALA SER PRO
SEQRES 39 A 520 GLU GLU LEU ARG ALA LEU GLU GLU ARG ASP ASN PRO PHE
SEQRES 40 A 520 PRO GLU ALA ASP PRO ARG LEU TYR LEU PHE ARG GLU ALA
MODRES 1UFA MSE A 1 MET SELENOMETHIONINE
MODRES 1UFA MSE A 20 MET SELENOMETHIONINE
MODRES 1UFA MSE A 32 MET SELENOMETHIONINE
MODRES 1UFA MSE A 185 MET SELENOMETHIONINE
MODRES 1UFA MSE A 213 MET SELENOMETHIONINE
MODRES 1UFA MSE A 432 MET SELENOMETHIONINE
MODRES 1UFA MSE A 450 MET SELENOMETHIONINE
MODRES 1UFA MSE A 465 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 20 8
HET MSE A 32 8
HET MSE A 185 8
HET MSE A 213 8
HET MSE A 432 8
HET MSE A 450 8
HET MSE A 465 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 HOH *296(H2 O)
HELIX 1 1 GLY A 24 THR A 35 1 12
HELIX 2 2 THR A 35 GLU A 49 1 15
HELIX 3 3 THR A 60 ALA A 68 1 9
HELIX 4 4 ASP A 69 ARG A 95 1 27
HELIX 5 5 LEU A 99 LEU A 120 1 22
HELIX 6 6 ASP A 123 GLY A 135 1 13
HELIX 7 7 TYR A 148 LEU A 152 5 5
HELIX 8 8 TYR A 154 ALA A 174 1 21
HELIX 9 9 LEU A 182 ALA A 186 5 5
HELIX 10 10 GLY A 207 ALA A 215 1 9
HELIX 11 11 ASP A 223 GLY A 229 1 7
HELIX 12 12 GLN A 247 HIS A 252 5 6
HELIX 13 13 ASN A 266 SER A 275 1 10
HELIX 14 14 GLY A 279 GLU A 283 5 5
HELIX 15 15 ASP A 309 LYS A 313 5 5
HELIX 16 16 ASP A 317 HIS A 343 1 27
HELIX 17 17 GLU A 355 PHE A 357 5 3
HELIX 18 18 GLU A 363 GLN A 377 1 15
HELIX 19 19 THR A 385 VAL A 390 1 6
HELIX 20 20 GLY A 405 ASP A 409 5 5
HELIX 21 21 ASN A 415 LYS A 417 5 3
HELIX 22 22 THR A 418 GLY A 439 1 22
HELIX 23 23 PRO A 442 GLU A 457 1 16
HELIX 24 24 SER A 459 GLY A 468 1 10
HELIX 25 25 ALA A 470 ALA A 492 1 23
HELIX 26 26 SER A 493 ASP A 504 1 12
HELIX 27 27 ASP A 511 LEU A 516 5 6
SHEET 1 A 5 PHE A 180 TRP A 181 0
SHEET 2 A 5 VAL A 137 SER A 142 1 N THR A 141 O TRP A 181
SHEET 3 A 5 PHE A 55 ILE A 59 1 N LEU A 57 O GLU A 138
SHEET 4 A 5 ALA A 2 ALA A 10 1 N ALA A 10 O GLY A 58
SHEET 5 A 5 VAL A 347 ASP A 353 1 O ILE A 348 N ARG A 3
SHEET 1 B 5 PHE A 180 TRP A 181 0
SHEET 2 B 5 VAL A 137 SER A 142 1 N THR A 141 O TRP A 181
SHEET 3 B 5 PHE A 55 ILE A 59 1 N LEU A 57 O GLU A 138
SHEET 4 B 5 ALA A 2 ALA A 10 1 N ALA A 10 O GLY A 58
SHEET 5 B 5 VAL A 381 PRO A 383 1 O ARG A 382 N PHE A 4
SHEET 1 C 2 GLY A 191 TRP A 193 0
SHEET 2 C 2 GLY A 203 ARG A 205 -1 O ARG A 205 N GLY A 191
SHEET 1 D 4 TYR A 219 VAL A 222 0
SHEET 2 D 4 ARG A 261 ALA A 264 1 O ARG A 261 N THR A 220
SHEET 3 D 4 HIS A 254 GLU A 255 -1 N HIS A 254 O VAL A 262
SHEET 4 D 4 VAL A 395 ARG A 396 1 O VAL A 395 N GLU A 255
SHEET 1 E 2 TRP A 301 ARG A 302 0
SHEET 2 E 2 ALA A 314 PRO A 315 -1 O ALA A 314 N ARG A 302
LINK C MSE A 1 N ALA A 2 1555 1555 1.33
LINK C GLY A 19 N MSE A 20 1555 1555 1.33
LINK C MSE A 20 N TRP A 21 1555 1555 1.33
LINK C ALA A 31 N MSE A 32 1555 1555 1.33
LINK C MSE A 32 N ALA A 33 1555 1555 1.33
LINK C GLU A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N ALA A 186 1555 1555 1.33
LINK C LEU A 212 N MSE A 213 1555 1555 1.33
LINK C MSE A 213 N ARG A 214 1555 1555 1.33
LINK C ALA A 431 N MSE A 432 1555 1555 1.33
LINK C MSE A 432 N ARG A 433 1555 1555 1.32
LINK C ALA A 449 N MSE A 450 1555 1555 1.33
LINK C MSE A 450 N ARG A 451 1555 1555 1.33
LINK C LEU A 464 N MSE A 465 1555 1555 1.33
LINK C MSE A 465 N GLU A 466 1555 1555 1.33
CISPEP 1 TRP A 21 PRO A 22 0 -0.11
CRYST1 119.376 119.376 73.898 90.00 90.00 90.00 P 42 21 2 8
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 0.008377 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013532 0.00000
HETATM 1 N MSE A 1 55.872 21.005 -5.528 1.00 66.02 N
HETATM 2 CA MSE A 1 56.225 22.314 -4.895 1.00 64.38 C
HETATM 3 C MSE A 1 56.504 22.166 -3.401 1.00 58.08 C
HETATM 4 O MSE A 1 55.582 21.949 -2.610 1.00 58.45 O
HETATM 5 CB MSE A 1 55.090 23.323 -5.099 1.00 70.55 C
HETATM 6 CG MSE A 1 53.709 22.792 -4.737 1.00 77.01 C
HETATM 7 SE MSE A 1 52.727 23.967 -3.552 1.00 87.22 SE
HETATM 8 CE MSE A 1 52.912 25.622 -4.540 1.00 83.71 C
(ATOM LINES ARE NOT SHOWN.)
END
