HEADER RNA BINDING PROTEIN 19-JUN-13 4LAB
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF RLUB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-251;
COMPND 5 SYNONYM: 23S RRNA PSEUDOURIDINE(2605) SYNTHASE, RRNA PSEUDOURIDYLATE
COMPND 6 SYNTHASE B, RRNA-URIDINE ISOMERASE B;
COMPND 7 EC: 5.4.99.22;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B1269, JW1261, RLUB, YCIL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET47 MODIFIED
KEYWDS BETA SHEET, ALPHA-BETA PROTEIN, PSEUDOURIDINE SYNTHASE, E. COLI
KEYWDS 2 RIBOSOMAL RNA, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.CZUDNOCHOWSKI,J.S.FINER-MOORE,R.M.STROUD
REVDAT 5 20-SEP-23 4LAB 1 REMARK SEQADV LINK
REVDAT 4 17-JUL-19 4LAB 1 REMARK
REVDAT 3 15-NOV-17 4LAB 1 REMARK
REVDAT 2 26-FEB-14 4LAB 1 JRNL
REVDAT 1 20-NOV-13 4LAB 0
JRNL AUTH N.CZUDNOCHOWSKI,G.W.ASHLEY,D.V.SANTI,A.ALIAN,J.FINER-MOORE,
JRNL AUTH 2 R.M.STROUD
JRNL TITL THE MECHANISM OF PSEUDOURIDINE SYNTHASES FROM A COVALENT
JRNL TITL 2 COMPLEX WITH RNA, AND ALTERNATE SPECIFICITY FOR U2605 VERSUS
JRNL TITL 3 U2604 BETWEEN CLOSE HOMOLOGS.
JRNL REF NUCLEIC ACIDS RES. V. 42 2037 2014
JRNL REFN ISSN 0305-1048
JRNL PMID 24214967
JRNL DOI 10.1093/NAR/GKT1050
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 9317
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 471
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 58.2743 - 3.6116 1.00 3058 176 0.2123 0.2362
REMARK 3 2 3.6116 - 2.8666 1.00 2921 147 0.2544 0.2974
REMARK 3 3 2.8666 - 2.5043 1.00 2867 148 0.2778 0.3198
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.20
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.50
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 : 0.006 1494
REMARK 3 ANGLE : 0.917 2029
REMARK 3 CHIRALITY : 0.060 225
REMARK 3 PLANARITY : 0.005 268
REMARK 3 DIHEDRAL : 14.750 553
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 65:138)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8883 8.8979 24.9800
REMARK 3 T TENSOR
REMARK 3 T11: 0.2672 T22: 0.4986
REMARK 3 T33: 0.2806 T12: 0.0526
REMARK 3 T13: 0.0007 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 3.9293 L22: 8.1207
REMARK 3 L33: 4.8960 L12: 2.7754
REMARK 3 L13: -0.0873 L23: -0.4351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0755 S12: 0.4765 S13: 0.0950
REMARK 3 S21: -0.4616 S22: 0.0403 S23: -0.3759
REMARK 3 S31: -0.0229 S32: 0.4250 S33: 0.0718
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 139:251)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3758 23.6706 27.2208
REMARK 3 T TENSOR
REMARK 3 T11: 0.3787 T22: 0.5422
REMARK 3 T33: 0.5803 T12: 0.0761
REMARK 3 T13: 0.1062 T23: 0.1086
REMARK 3 L TENSOR
REMARK 3 L11: 1.0967 L22: 4.9251
REMARK 3 L33: 4.4886 L12: 0.5513
REMARK 3 L13: -0.7487 L23: -3.0206
REMARK 3 S TENSOR
REMARK 3 S11: 0.1668 S12: 0.1774 S13: 0.3592
REMARK 3 S21: 0.4264 S22: 0.2178 S23: 0.6725
REMARK 3 S31: -0.6925 S32: -0.6268 S33: -0.3311
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 4LAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.068830
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 58.259
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 18.90
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 17.50
REMARK 200 R MERGE FOR SHELL (I) : 1.53000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2GML
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.6, 20%
REMARK 280 ISOPROPANOL, 15% PEG4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 37.45000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.19500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.19500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.17500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.19500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.19500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 18.72500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.19500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.19500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.17500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.19500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.19500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 18.72500
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 37.45000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 LEU A 5
REMARK 465 GLN A 6
REMARK 465 LYS A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 ARG A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 HIS A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 ARG A 17
REMARK 465 ARG A 18
REMARK 465 GLU A 19
REMARK 465 ILE A 20
REMARK 465 GLU A 21
REMARK 465 SER A 22
REMARK 465 ILE A 23
REMARK 465 ILE A 24
REMARK 465 GLU A 25
REMARK 465 ALA A 26
REMARK 465 GLY A 27
REMARK 465 ARG A 28
REMARK 465 VAL A 29
REMARK 465 SER A 30
REMARK 465 VAL A 31
REMARK 465 ASP A 32
REMARK 465 GLY A 33
REMARK 465 LYS A 34
REMARK 465 ILE A 35
REMARK 465 ALA A 36
REMARK 465 LYS A 37
REMARK 465 LEU A 38
REMARK 465 GLY A 39
REMARK 465 ASP A 40
REMARK 465 ARG A 41
REMARK 465 VAL A 42
REMARK 465 GLU A 43
REMARK 465 VAL A 44
REMARK 465 THR A 45
REMARK 465 PRO A 46
REMARK 465 GLY A 47
REMARK 465 LEU A 48
REMARK 465 LYS A 49
REMARK 465 ILE A 50
REMARK 465 ARG A 51
REMARK 465 ILE A 52
REMARK 465 ASP A 53
REMARK 465 GLY A 54
REMARK 465 HIS A 55
REMARK 465 LEU A 56
REMARK 465 ILE A 57
REMARK 465 SER A 58
REMARK 465 VAL A 59
REMARK 465 ARG A 60
REMARK 465 GLU A 61
REMARK 465 SER A 62
REMARK 465 ALA A 63
REMARK 465 GLU A 64
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 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 161 CD OE1 NE2
REMARK 470 LYS A 170 CG CD CE NZ
REMARK 470 ARG A 194 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 209 CD NE CZ NH1 NH2
REMARK 470 LYS A 222 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 PRO A 85 2.90 -67.54
REMARK 500 SER A 175 -142.36 -86.25
REMARK 500 GLU A 190 -149.36 -88.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PT A 301 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 114 SG
REMARK 620 2 ARG A 226 NH2 66.9
REMARK 620 3 ARG A 226 NE 98.2 52.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303
DBREF 4LAB A 1 251 UNP P37765 RLUB_ECOLI 1 251
SEQADV 4LAB GLY A -3 UNP P37765 EXPRESSION TAG
SEQADV 4LAB PRO A -2 UNP P37765 EXPRESSION TAG
SEQADV 4LAB GLY A -1 UNP P37765 EXPRESSION TAG
SEQADV 4LAB SER A 0 UNP P37765 EXPRESSION TAG
SEQRES 1 A 255 GLY PRO GLY SER MET SER GLU LYS LEU GLN LYS VAL LEU
SEQRES 2 A 255 ALA ARG ALA GLY HIS GLY SER ARG ARG GLU ILE GLU SER
SEQRES 3 A 255 ILE ILE GLU ALA GLY ARG VAL SER VAL ASP GLY LYS ILE
SEQRES 4 A 255 ALA LYS LEU GLY ASP ARG VAL GLU VAL THR PRO GLY LEU
SEQRES 5 A 255 LYS ILE ARG ILE ASP GLY HIS LEU ILE SER VAL ARG GLU
SEQRES 6 A 255 SER ALA GLU GLN ILE CYS ARG VAL LEU ALA TYR TYR LYS
SEQRES 7 A 255 PRO GLU GLY GLU LEU CYS THR ARG ASN ASP PRO GLU GLY
SEQRES 8 A 255 ARG PRO THR VAL PHE ASP ARG LEU PRO LYS LEU ARG GLY
SEQRES 9 A 255 ALA ARG TRP ILE ALA VAL GLY ARG LEU ASP VAL ASN THR
SEQRES 10 A 255 CYS GLY LEU LEU LEU PHE THR THR ASP GLY GLU LEU ALA
SEQRES 11 A 255 ASN ARG LEU MET HIS PRO SER ARG GLU VAL GLU ARG GLU
SEQRES 12 A 255 TYR ALA VAL ARG VAL PHE GLY GLN VAL ASP ASP ALA LYS
SEQRES 13 A 255 LEU ARG ASP LEU SER ARG GLY VAL GLN LEU GLU ASP GLY
SEQRES 14 A 255 PRO ALA ALA PHE LYS THR ILE LYS PHE SER GLY GLY GLU
SEQRES 15 A 255 GLY ILE ASN GLN TRP TYR ASN VAL THR LEU THR GLU GLY
SEQRES 16 A 255 ARG ASN ARG GLU VAL ARG ARG LEU TRP GLU ALA VAL GLY
SEQRES 17 A 255 VAL GLN VAL SER ARG LEU ILE ARG VAL ARG TYR GLY ASP
SEQRES 18 A 255 ILE PRO LEU PRO LYS GLY LEU PRO ARG GLY GLY TRP THR
SEQRES 19 A 255 GLU LEU ASP LEU ALA GLN THR ASN TYR LEU ARG GLU LEU
SEQRES 20 A 255 VAL GLU LEU PRO PRO GLU THR SER
HET PT A 301 1
HET PT A 302 1
HET CL A 303 1
HETNAM PT PLATINUM (II) ION
HETNAM CL CHLORIDE ION
FORMUL 2 PT 2(PT 2+)
FORMUL 4 CL CL 1-
FORMUL 5 HOH *19(H2 O)
HELIX 1 1 ASP A 122 HIS A 131 1 10
HELIX 2 2 ASP A 149 GLY A 159 1 11
HELIX 3 3 ARG A 194 ALA A 202 1 9
HELIX 4 4 ASP A 233 LEU A 243 1 11
SHEET 1 A 4 ILE A 104 ALA A 105 0
SHEET 2 A 4 CYS A 114 THR A 120 -1 O THR A 120 N ILE A 104
SHEET 3 A 4 VAL A 207 TYR A 215 1 O LEU A 210 N CYS A 114
SHEET 4 A 4 ILE A 218 PRO A 219 -1 O ILE A 218 N TYR A 215
SHEET 1 B 7 THR A 171 GLU A 178 0
SHEET 2 B 7 ASN A 181 LEU A 188 -1 O ASN A 185 N LYS A 173
SHEET 3 B 7 ARG A 138 VAL A 144 -1 N VAL A 142 O TYR A 184
SHEET 4 B 7 VAL A 207 TYR A 215 -1 O ILE A 211 N ALA A 141
SHEET 5 B 7 CYS A 114 THR A 120 1 N CYS A 114 O LEU A 210
SHEET 6 B 7 VAL A 69 LYS A 74 -1 N LYS A 74 O GLY A 115
SHEET 7 B 7 TRP A 229 GLU A 231 -1 O THR A 230 N ALA A 71
SHEET 1 C 2 VAL A 160 LEU A 162 0
SHEET 2 C 2 GLY A 165 ALA A 167 -1 O ALA A 167 N VAL A 160
LINK SG CYS A 114 PT PT A 301 1555 1555 2.45
LINK SD MET A 130 PT PT A 302 1555 1555 2.52
LINK NH2 ARG A 226 PT PT A 301 1555 1555 2.41
LINK NE ARG A 226 PT PT A 301 1555 1555 2.76
SITE 1 AC1 4 CYS A 114 ARG A 209 ARG A 226 CL A 303
SITE 1 AC2 3 GLY A 107 MET A 130 TRP A 229
SITE 1 AC3 2 ARG A 209 PT A 301
CRYST1 82.390 82.390 74.900 90.00 90.00 90.00 P 43 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 0.012137 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012137 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
