HEADER TRANSFERASE 22-MAR-13 4JT4
TITLE STRUCTURE OF CLOSTRIDIUM THERMOCELLUM POLYNUCLEOTIDE KINASE BOUND TO
TITLE 2 DATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOPHOSPHOESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.1.78;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 203119;
SOURCE 4 STRAIN: ATCC 27405 / DSM 1237;
SOURCE 5 GENE: CTHE_2768;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RNA REPAIR, P-LOOP PHOSPHOTRANSFERASE, POLYNUCLEOTIDE KINASE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.DAS,L.K.WANG,P.SMITH,S.SHUMAN
REVDAT 2 18-DEC-13 4JT4 1 JRNL
REVDAT 1 28-AUG-13 4JT4 0
JRNL AUTH U.DAS,L.K.WANG,P.SMITH,S.SHUMAN
JRNL TITL STRUCTURAL AND BIOCHEMICAL ANALYSIS OF THE PHOSPHATE DONOR
JRNL TITL 2 SPECIFICITY OF THE POLYNUCLEOTIDE KINASE COMPONENT OF THE
JRNL TITL 3 BACTERIAL PNKPHEN1 RNA REPAIR SYSTEM.
JRNL REF BIOCHEMISTRY V. 52 4734 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23721485
JRNL DOI 10.1021/BI400412X
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 24307
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.880
REMARK 3 FREE R VALUE TEST SET COUNT : 1916
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 44.5490 - 4.8490 0.99 1760 150 0.1814 0.2271
REMARK 3 2 4.8490 - 3.8495 1.00 1668 143 0.1333 0.1847
REMARK 3 3 3.8495 - 3.3631 1.00 1647 141 0.1434 0.2047
REMARK 3 4 3.3631 - 3.0557 1.00 1630 140 0.1561 0.2218
REMARK 3 5 3.0557 - 2.8367 0.99 1620 139 0.1613 0.2055
REMARK 3 6 2.8367 - 2.6695 1.00 1604 138 0.1545 0.2286
REMARK 3 7 2.6695 - 2.5358 0.99 1621 139 0.1679 0.2463
REMARK 3 8 2.5358 - 2.4254 0.99 1627 140 0.1625 0.2686
REMARK 3 9 2.4254 - 2.3320 1.00 1604 136 0.1640 0.2602
REMARK 3 10 2.3320 - 2.2516 0.99 1568 136 0.1449 0.2158
REMARK 3 11 2.2516 - 2.1812 0.99 1596 138 0.1390 0.1974
REMARK 3 12 2.1812 - 2.1188 0.99 1596 135 0.1382 0.2172
REMARK 3 13 2.1188 - 2.0630 0.99 1573 135 0.1487 0.2006
REMARK 3 14 2.0630 - 2.0100 0.80 1277 106 0.1513 0.2544
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.300
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 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 : 0.010 2876
REMARK 3 ANGLE : 1.273 3894
REMARK 3 CHIRALITY : 0.078 437
REMARK 3 PLANARITY : 0.006 492
REMARK 3 DIHEDRAL : 16.235 1122
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4JT4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078470.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 130
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24363
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 45.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -999.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
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) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT REFINEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, 100MM MGCL2, 16-
REMARK 280 18% PEG 3350, 2MM DATP, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 22.65300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.77300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.39050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.77300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.65300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.39050
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU B 167 O HOH B 418 2.13
REMARK 500 O HOH B 434 O HOH B 438 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP A 96 O HOH A 394 3656 2.18
REMARK 500 NZ LYS B 118 O HOH B 439 1455 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 ASN B 49 40.66 -109.98
REMARK 500 GLN B 169 -64.03 -104.72
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 MG A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DTP A 202 O3G
REMARK 620 2 DTP A 202 O2B 88.6
REMARK 620 3 SER A 22 OG 173.6 89.5
REMARK 620 4 HOH A 303 O 90.1 178.1 91.7
REMARK 620 5 HOH A 301 O 85.9 94.6 88.2 83.8
REMARK 620 6 HOH A 304 O 91.7 87.7 94.3 93.8 176.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DTP B 202 O3G
REMARK 620 2 DTP B 202 O1B 96.2
REMARK 620 3 SER B 22 OG 172.4 89.4
REMARK 620 4 HOH B 305 O 91.6 91.5 93.4
REMARK 620 5 HOH B 303 O 91.5 93.0 83.1 174.2
REMARK 620 6 HOH B 306 O 89.3 173.4 84.8 92.1 83.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 355 O
REMARK 620 2 HOH B 352 O 96.8
REMARK 620 3 HOH B 388 O 137.6 112.9
REMARK 620 4 HOH B 372 O 81.8 72.8 79.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTP A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTP B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JST RELATED DB: PDB
REMARK 900 RELATED ID: 4JSY RELATED DB: PDB
REMARK 900 RELATED ID: 4JT2 RELATED DB: PDB
REMARK 900 RELATED ID: 4GP7 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH ATP
REMARK 900 RELATED ID: 4GP6 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH ADP
DBREF 4JT4 A 1 170 UNP A3DJ38 A3DJ38_CLOTH 1 170
DBREF 4JT4 B 1 170 UNP A3DJ38 A3DJ38_CLOTH 1 170
SEQADV 4JT4 SER A 0 UNP A3DJ38 EXPRESSION TAG
SEQADV 4JT4 MSE A 44 UNP A3DJ38 VAL 44 ENGINEERED MUTATION
SEQADV 4JT4 MSE A 137 UNP A3DJ38 LEU 137 ENGINEERED MUTATION
SEQADV 4JT4 SER B 0 UNP A3DJ38 EXPRESSION TAG
SEQADV 4JT4 MSE B 44 UNP A3DJ38 VAL 44 ENGINEERED MUTATION
SEQADV 4JT4 MSE B 137 UNP A3DJ38 LEU 137 ENGINEERED MUTATION
SEQRES 1 A 171 SER MSE LYS LEU THR ILE PRO GLU LEU SER LEU VAL VAL
SEQRES 2 A 171 LEU ILE GLY SER SER GLY SER GLY LYS SER THR PHE ALA
SEQRES 3 A 171 LYS LYS HIS PHE LYS PRO THR GLU VAL ILE SER SER ASP
SEQRES 4 A 171 PHE CYS ARG GLY LEU MSE SER ASP ASP GLU ASN ASP GLN
SEQRES 5 A 171 THR VAL THR GLY ALA ALA PHE ASP VAL LEU HIS TYR ILE
SEQRES 6 A 171 VAL SER LYS ARG LEU GLN LEU GLY LYS LEU THR VAL VAL
SEQRES 7 A 171 ASP ALA THR ASN VAL GLN GLU SER ALA ARG LYS PRO LEU
SEQRES 8 A 171 ILE GLU ILE ALA LYS ASP TYR HIS CYS PHE PRO VAL ALA
SEQRES 9 A 171 VAL VAL PHE ASN LEU PRO GLU LYS VAL CYS GLN GLU ARG
SEQRES 10 A 171 ASN LYS ASN ARG THR ASP ARG GLN VAL GLU GLU TYR VAL
SEQRES 11 A 171 ILE ARG LYS HIS THR GLN GLN MSE LYS LYS SER ILE LYS
SEQRES 12 A 171 GLY LEU GLN ARG GLU GLY PHE ARG TYR VAL TYR ILE LEU
SEQRES 13 A 171 ASN SER PRO GLU GLU VAL GLU GLU VAL VAL PHE GLU ARG
SEQRES 14 A 171 GLN PRO
SEQRES 1 B 171 SER MSE LYS LEU THR ILE PRO GLU LEU SER LEU VAL VAL
SEQRES 2 B 171 LEU ILE GLY SER SER GLY SER GLY LYS SER THR PHE ALA
SEQRES 3 B 171 LYS LYS HIS PHE LYS PRO THR GLU VAL ILE SER SER ASP
SEQRES 4 B 171 PHE CYS ARG GLY LEU MSE SER ASP ASP GLU ASN ASP GLN
SEQRES 5 B 171 THR VAL THR GLY ALA ALA PHE ASP VAL LEU HIS TYR ILE
SEQRES 6 B 171 VAL SER LYS ARG LEU GLN LEU GLY LYS LEU THR VAL VAL
SEQRES 7 B 171 ASP ALA THR ASN VAL GLN GLU SER ALA ARG LYS PRO LEU
SEQRES 8 B 171 ILE GLU ILE ALA LYS ASP TYR HIS CYS PHE PRO VAL ALA
SEQRES 9 B 171 VAL VAL PHE ASN LEU PRO GLU LYS VAL CYS GLN GLU ARG
SEQRES 10 B 171 ASN LYS ASN ARG THR ASP ARG GLN VAL GLU GLU TYR VAL
SEQRES 11 B 171 ILE ARG LYS HIS THR GLN GLN MSE LYS LYS SER ILE LYS
SEQRES 12 B 171 GLY LEU GLN ARG GLU GLY PHE ARG TYR VAL TYR ILE LEU
SEQRES 13 B 171 ASN SER PRO GLU GLU VAL GLU GLU VAL VAL PHE GLU ARG
SEQRES 14 B 171 GLN PRO
MODRES 4JT4 MSE A 1 MET SELENOMETHIONINE
MODRES 4JT4 MSE A 44 MET SELENOMETHIONINE
MODRES 4JT4 MSE A 137 MET SELENOMETHIONINE
MODRES 4JT4 MSE B 1 MET SELENOMETHIONINE
MODRES 4JT4 MSE B 44 MET SELENOMETHIONINE
MODRES 4JT4 MSE B 137 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 44 8
HET MSE A 137 8
HET MSE B 1 8
HET MSE B 44 8
HET MSE B 137 8
HET MG A 201 1
HET DTP A 202 30
HET MG B 201 1
HET DTP B 202 30
HET NA B 203 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
HETNAM NA SODIUM ION
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 MG 2(MG 2+)
FORMUL 4 DTP 2(C10 H16 N5 O12 P3)
FORMUL 7 NA NA 1+
FORMUL 8 HOH *279(H2 O)
HELIX 1 1 GLY A 20 PHE A 29 1 10
HELIX 2 2 LYS A 30 THR A 32 5 3
HELIX 3 3 SER A 37 SER A 45 1 9
HELIX 4 4 ASP A 50 THR A 52 5 3
HELIX 5 5 VAL A 53 LEU A 71 1 19
HELIX 6 6 GLN A 83 TYR A 97 1 15
HELIX 7 7 PRO A 109 ASN A 119 1 11
HELIX 8 8 GLU A 126 ILE A 141 1 16
HELIX 9 9 GLY A 143 GLY A 148 1 6
HELIX 10 10 SER A 157 GLU A 163 1 7
HELIX 11 11 GLY B 20 PHE B 29 1 10
HELIX 12 12 LYS B 30 THR B 32 5 3
HELIX 13 13 SER B 37 SER B 45 1 9
HELIX 14 14 VAL B 53 LEU B 71 1 19
HELIX 15 15 GLN B 83 TYR B 97 1 15
HELIX 16 16 PRO B 109 ARG B 120 1 12
HELIX 17 17 GLU B 126 ILE B 141 1 16
HELIX 18 18 GLY B 143 GLY B 148 1 6
HELIX 19 19 SER B 157 GLU B 163 1 7
SHEET 1 A 2 MSE A 1 PRO A 6 0
SHEET 2 A 2 VAL A 164 GLN A 169 1 O GLU A 167 N LEU A 3
SHEET 1 B 5 VAL A 34 SER A 36 0
SHEET 2 B 5 THR A 75 ASP A 78 1 O VAL A 76 N ILE A 35
SHEET 3 B 5 SER A 9 ILE A 14 1 N VAL A 11 O VAL A 77
SHEET 4 B 5 PHE A 100 PHE A 106 1 O PHE A 106 N ILE A 14
SHEET 5 B 5 TYR A 151 LEU A 155 1 O TYR A 153 N VAL A 105
SHEET 1 C 2 MSE B 1 ILE B 5 0
SHEET 2 C 2 VAL B 164 ARG B 168 1 O GLU B 167 N ILE B 5
SHEET 1 D 5 VAL B 34 SER B 36 0
SHEET 2 D 5 THR B 75 ASP B 78 1 O VAL B 76 N ILE B 35
SHEET 3 D 5 SER B 9 ILE B 14 1 N VAL B 11 O VAL B 77
SHEET 4 D 5 PHE B 100 PHE B 106 1 O VAL B 102 N VAL B 12
SHEET 5 D 5 TYR B 151 LEU B 155 1 O LEU B 155 N VAL B 105
LINK C SER A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C LEU A 43 N MSE A 44 1555 1555 1.33
LINK C MSE A 44 N SER A 45 1555 1555 1.33
LINK C GLN A 136 N MSE A 137 1555 1555 1.33
LINK C MSE A 137 N LYS A 138 1555 1555 1.33
LINK C SER B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C LEU B 43 N MSE B 44 1555 1555 1.33
LINK C MSE B 44 N SER B 45 1555 1555 1.33
LINK C GLN B 136 N MSE B 137 1555 1555 1.33
LINK C MSE B 137 N LYS B 138 1555 1555 1.32
LINK MG MG A 201 O3G DTP A 202 1555 1555 1.91
LINK MG MG B 201 O3G DTP B 202 1555 1555 1.96
LINK MG MG B 201 O1B DTP B 202 1555 1555 1.98
LINK MG MG A 201 O2B DTP A 202 1555 1555 2.04
LINK OG SER A 22 MG MG A 201 1555 1555 2.07
LINK OG SER B 22 MG MG B 201 1555 1555 2.17
LINK MG MG A 201 O HOH A 303 1555 1555 2.04
LINK MG MG B 201 O HOH B 305 1555 1555 2.10
LINK MG MG B 201 O HOH B 303 1555 1555 2.11
LINK MG MG A 201 O HOH A 301 1555 1555 2.13
LINK MG MG A 201 O HOH A 304 1555 1555 2.17
LINK MG MG B 201 O HOH B 306 1555 1555 2.26
LINK NA NA B 203 O HOH B 355 1555 1555 3.00
LINK NA NA B 203 O HOH B 352 1555 1555 3.05
LINK NA NA B 203 O HOH B 388 1555 1555 3.10
LINK NA NA B 203 O HOH B 372 1555 1555 3.16
SITE 1 AC1 5 SER A 22 DTP A 202 HOH A 301 HOH A 303
SITE 2 AC1 5 HOH A 304
SITE 1 AC2 22 SER A 16 SER A 17 GLY A 18 SER A 19
SITE 2 AC2 22 GLY A 20 LYS A 21 SER A 22 THR A 23
SITE 3 AC2 22 ARG A 116 ARG A 120 ARG A 123 MG A 201
SITE 4 AC2 22 HOH A 301 HOH A 303 HOH A 304 HOH A 341
SITE 5 AC2 22 HOH A 348 HOH A 368 HOH A 375 HOH A 377
SITE 6 AC2 22 HOH A 391 HOH A 395
SITE 1 AC3 5 SER B 22 DTP B 202 HOH B 303 HOH B 305
SITE 2 AC3 5 HOH B 306
SITE 1 AC4 21 SER B 16 SER B 17 GLY B 18 SER B 19
SITE 2 AC4 21 GLY B 20 LYS B 21 SER B 22 THR B 23
SITE 3 AC4 21 ARG B 116 ARG B 120 MG B 201 HOH B 303
SITE 4 AC4 21 HOH B 305 HOH B 306 HOH B 330 HOH B 338
SITE 5 AC4 21 HOH B 344 HOH B 347 HOH B 355 HOH B 367
SITE 6 AC4 21 HOH B 424
SITE 1 AC5 4 PHE B 24 HOH B 352 HOH B 355 HOH B 388
CRYST1 45.306 66.781 119.546 90.00 90.00 90.00 P 21 21 21 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 0.022072 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014974 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008365 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
